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356  structures 1582  species 0  interactions 61809  sequences 1091  architectures

Family: Kinesin (PF00225)

Summary: Kinesin motor domain

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The kinesin dimer (red) attaches to, and moves along, microtubules (blue and green).
Animation of kinesin "walking" on a microtubule

A kinesin is a protein belonging to a class of motor proteins found in eukaryotic cells.

Kinesins move along microtubule (MT) filaments, and are powered by the hydrolysis of adenosine triphosphate (ATP) (thus kinesins are ATPases, a type of enzyme). The active movement of kinesins supports several cellular functions including mitosis, meiosis and transport of cellular cargo, such as in axonal transport. Most kinesins walk towards the plus end of a microtubule, which, in most cells, entails transporting cargo such as protein and membrane components from the center of the cell towards the periphery.[1] This form of transport is known as anterograde transport. In contrast, dyneins are motor proteins that move toward the minus end of a microtubule in retrograde transport.


Kinesins were discovered in 1985, based on their motility in cytoplasm extruded from the giant axon of the squid.[2]

They turned out as MT-based anterograde intracellular transport motors.[3] The founding member of this superfamily, kinesin-1, was isolated as a heterotetrameric fast axonal organelle transport motor consisting of 2 identical motor subunits (KHC) and 2 "light chains" (KLC) via microtubule affinity purification from neuronal cell extracts.[4] Subsequently, a different, heterotrimeric plus-end-directed MT-based motor named kinesin-2, consisting of 2 distinct KHC-related motor subunits and an accessory "KAP" subunit, was purified from echinoderm egg/embryo extracts[5] and is best known for its role in transporting protein complexes (IFT particles) along axonemes during cilium biogenesis.[6] Molecular genetic and genomic approaches have led to the recognition that the kinesins form a diverse superfamily of motors that are responsible for multiple intracellular motility events in eukaryotic cells.[7][8][9][10] For example, the genomes of mammals encode more than 40 kinesin proteins,[11] organized into at least 14 families named kinesin-1 through kinesin-14.[12]


Overall structure

Members of the kinesin superfamily vary in shape but the prototypical kinesin-1 motor consists of two Kinesin Heavy Chain (KHC) molecules which form a protein dimer (molecule pair) that binds two light chains (KLCs), which are unique for different cargos.

The heavy chain of kinesin-1 comprises a globular head (the motor domain) at the amino terminal end connected via a short, flexible neck linker to the stalk – a long, central alpha-helical coiled coil domain – that ends in a carboxy terminal tail domain which associates with the light-chains. The stalks of two KHCs intertwine to form a coiled coil that directs dimerization of the two KHCs. In most cases transported cargo binds to the kinesin light chains, at the TPR motif sequence of the KLC, but in some cases cargo binds to the C-terminal domains of the heavy chains.[13]

Kinesin motor domain

Kinesin motor domain
Kinesin motor domain 1BG2.png
Crystallographic structure of the human kinesin motor domain depicted as a rainbow colored cartoon (N-terminus = blue, C-terminus = red) complexed with ADP (stick diagram, carbon = white, oxygen = red, nitrogen = blue, phosphorus = orange) and a magnesium ion (grey sphere).[14]
SymbolKinesin motor domain

The head is the signature of kinesin and its amino acid sequence is well conserved among various kinesins. Each head has two separate binding sites: one for the microtubule and the other for ATP. ATP binding and hydrolysis as well as ADP release change the conformation of the microtubule-binding domains and the orientation of the neck linker with respect to the head; this results in the motion of the kinesin. Several structural elements in the Head, including a central beta-sheet domain and the Switch I and II domains, have been implicated as mediating the interactions between the two binding sites and the neck domain. Kinesins are structurally related to G proteins, which hydrolyze GTP instead of ATP. Several structural elements are shared between the two families, notably the Switch I and Switch II domain.

Mobile and self-inhibited conformations of kinesin-1. Self-inhibited conformation:IAK region of the tail (green) binds to motor domains (yellow and orange) to inhibit the enzymatic cycle of kinesin-1.Mobile conformation: Absent the tail binding, kinesin-1 motor domains (yellow and orange) can move freely along the microtubule(MT).[15] PDB 2Y65; PDB 2Y5W.
Detailed view of kinesin-1 self-inhibition (one of two possible conformations shown). Highlight: positively charged residues (blue) of the IAK region interact at multiple locations with negatively charged residues (red) of the motor domains[15] PDB 2Y65

Basic kinesin regulation

Kinesins tend to have low basal enzymatic activity which becomes significant when microtubule-activated.[16] In addition, many members of the kinesin superfamily can be self-inhibited by the binding of tail domain to the motor domain.[17] Such self-inhibition can then be relieved via additional regulation such as binding to cargo or cargo adapters.[18][19]

Cargo transport

In the cell, small molecules, such as gases and glucose, diffuse to where they are needed. Large molecules synthesised in the cell body, intracellular components such as vesicles and organelles such as mitochondria are too large (and the cytosol too crowded) to be able to diffuse to their destinations. Motor proteins fulfill the role of transporting large cargo about the cell to their required destinations. Kinesins are motor proteins that transport such cargo by walking unidirectionally along microtubule tracks hydrolysing one molecule of adenosine triphosphate (ATP) at each step.[20] It was thought that ATP hydrolysis powered each step, the energy released propelling the head forwards to the next binding site.[21] However, it has been proposed that the head diffuses forward and the force of binding to the microtubule is what pulls the cargo along.[22] In addition viruses, HIV for example, exploit kinesins to allow virus particle shuttling after assembly.[23]

There is significant evidence that cargoes in-vivo are transported by multiple motors.[24][25][26][27]

Direction of motion

Motor proteins travel in a specific direction along a microtubule. Microtubules are polar; meaning, the heads only bind to the microtubule in one orientation, while ATP binding gives each step its direction through a process known as neck linker zippering.[28]

It has been previously known that kinesin move cargo towards the plus (+) end of a microtubule, also known as anterograde transport/orthograde transport.[29] However, it has been recently discovered that in budding yeast cells kinesin Cin8 (a member of the Kinesin-5 family) can move toward the minus end as well, or retrograde transport. This means, these unique yeast kinesin homotetramers have the novel ability to move bi-directionally.[30][31][32] Kinesin, so far, has only been shown to move toward the minus end when in a group, with motors sliding in the antiparallel direction in an attempt to separate microtubules.[33] This dual directionality has been observed in identical conditions where free Cin8 molecules move towards the minus end, but cross-linking Cin8 move toward the plus ends of each cross-linked microtubule. One specific study tested the speed at which Cin8 motors moved, their results yielded a range of about 25-55 nm/s, in the direction of the spindle poles.[34] On an individual basis it has been found that by varying ionic conditions Cin8 motors can become as fast as 380 nm/s.[34] It is suggested that the bidirectionality of yeast kinesin-5 motors such as Cin8 and Cut7 is a result of coupling with other Cin8 motors and helps to fulfill the role of dynein in budding yeast, as opposed to the human homologue of these motors, the plus directed Eg5.[35] This discovery in kinesin-14 family proteins (such as Drosophila melanogaster NCD, budding yeast KAR3, and Arabidopsis thaliana ATK5) allows kinesin to walk in the opposite direction, toward microtubule minus end.[36] This is not typical of kinesin, rather, an exception to the normal direction of movement.

Diagram illustrating motility of kinesin.

Another type of motor protein, known as dyneins, move towards the minus end of the microtubule. Thus, they transport cargo from the periphery of the cell towards the center. An example of this would be transport occurring from the terminal boutons of a neuronal axon to the cell body (soma). This is known as retrograde transport.

Proposed mechanisms of movement

Kinesin accomplishes transport by "walking" along a microtubule. Two mechanisms have been proposed to account for this movement.

  • In the "hand-over-hand" mechanism, the kinesin heads step past one another, alternating the lead position.
  • In the "inchworm" mechanism, one kinesin head always leads, moving forward a step before the trailing head catches up.

Despite some remaining controversy, mounting experimental evidence points towards the hand-over-hand mechanism as being more likely.[37][38]

ATP binding and hydrolysis cause kinesin to travel via a "seesaw mechanism" about a pivot point.[39][40] This seesaw mechanism accounts for observations that the binding of the ATP to the no-nucleotide, microtubule-bound state results in a tilting of the kinesin motor domain relative to the microtubule. Critically, prior to this tilting the neck linker is unable to adopt its motor-head docked, forward-facing conformation. The ATP-induced tilting provides the opportunity for the neck linker to dock in this forward-facing conformation. This model is based on CRYO-EM models of the microtubule-bound kinesin structure which represent the beginning and end states of the process, but cannot resolve the precise details of the transition between the structures.

Theoretical modeling

A number of theoretical models of the molecular motor protein kinesin have been proposed.[41][42][43] Many challenges are encountered in theoretical investigations given the remaining uncertainties about the roles of protein structures, the precise way energy from ATP is transformed into mechanical work, and the roles played by thermal fluctuations. This is a rather active area of research. There is a need especially for approaches which better make a link with the molecular architecture of the protein and data obtained from experimental investigations.

The single-molecule dynamics are already well described[44] but it seems that these nano scale machines typically work in large teams.

Single-molecule dynamics are based on the distinct chemical states of the motor and observations about its mechanical steps.[45] For small concentrations of adenosine diphosphate, the motor’s behaviour is governed by the competition of two chemomechanical motor cycles which determine the motor’s stall force. A third cycle becomes important for large ADP concentrations.[45] Models with a single cycle have been discussed too. Seiferth et al. demonstrated how quantities such as the velocity or the entropy production of a motor change when adjacent states are merged in a multi-cyclic model until eventually the number of cycles is reduced.[46]

Recent experimental research has shown that kinesins, while moving along microtubules, interact with each other,[47][48] the interactions being short range and weak attractive (1.6±0.5 KBT). One model that has been developed takes into account these particle interactions,[44] where the dynamic rates change accordingly with the energy of interaction. If the energy is positive the rate of creating bonds (q) will be higher while the rate of breaking bonds (r) will be lower. One can understand that the rates of entrance and exit in the microtubule will be changed as well by the energy (See figure 1 in reference 30). If the second site is occupied the rate of entrance will be α*q and if the last but one site is occupied the rate of exit will be β*r. This theoretical approach agrees with the results of Monte Carlo simulations for this model, especially for the limiting case of very large negative energy. The normal totally asymmetric simple exclusion process for (or TASEP) results can be recovered from this model making the energy equal to zero.


In recent years, it has been found that microtubule-based molecular motors (including a number of kinesins) have a role in mitosis (cell division). Kinesins are important for proper spindle length and are involved in sliding microtubules apart within the spindle during prometaphase and metaphase, as well as depolymerizing microtubule minus ends at centrosomes during anaphase.[49] Specifically, Kinesin-5 family proteins act within the spindle to slide microtubules apart, while the Kinesin 13 family act to depolymerize microtubules.

Kinesin superfamily members

Human kinesin superfamily members include the following proteins, which in the standardized nomenclature developed by the community of kinesin researchers, are organized into 14 families named kinesin-1 through kinesin-14:[12]

  • 1A – KIF1A, 1B – KIF1B, 1C – KIF1C = kinesin-3
  • 2A – KIF2A, 2C – KIF2C = kinesin-13
  • 3B – KIF3B or 3C – KIF3C ,3A - KIF3A = kinesin-2
  • 4A – KIF4A, 4B – KIF4B = kinesin-4
  • 5A – KIF5A, 5B – KIF5B, 5C – KIF5C = kinesin-1
  • 6 – KIF6 = kinesin-9
  • 7 – KIF7 = kinesin-4
  • 9 – KIF9 = kinesin-9
  • 11 – KIF11 = kinesin-5
  • 12 – KIF12 = kinesin-12
  • 13A – KIF13A, 13B – KIF13B = kinesin-3
  • 14 – KIF14 = kinesin-3
  • 15 – KIF15 = kinesin-12
  • 16B – KIF16B = kinesin-3
  • 17 – KIF17 = kinesin-2
  • 18A – KIF18A, 18B – KIF18B = kinesin-8
  • 19 – KIF19 = kinesin-8
  • 20A – KIF20A, 20B – KIF20B = kinesin-6
  • 21A – KIF21A, 21B – KIF21B = kinesin-4
  • 22 – KIF22 = kinesin-10
  • 23 – KIF23 = kinesin-6
  • 24 – KIF24 = kinesin-13
  • 25 – KIF25 = kinesin-14
  • 26A – KIF26A, 26B – KIF26B = kinesin-11
  • 27 – KIF27 = kinesin-4
  • C1 – KIFC1, C2 – KIFC2, C3 – KIFC3 = kinesin-14

kinesin-1 light chains:

kinesin-2 associated protein:

  • KIFAP3 (also known as KAP-1, KAP3)

See also


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  49. ^ Goshima G, Vale RD (August 2005). "Cell cycle-dependent dynamics and regulation of mitotic kinesins in Drosophila S2 cells". Molecular Biology of the Cell. 16 (8): 3896–907. doi:10.1091/mbc.E05-02-0118. PMC 1182325. PMID 15958489.

Further reading

  • Lawrence CJ, Dawe RK, Christie KR, Cleveland DW, Dawson SC, Endow SA, Goldstein LS, Goodson HV, Hirokawa N, Howard J, Malmberg RL, McIntosh JR, Miki H, Mitchison TJ, Okada Y, Reddy AS, Saxton WM, Schliwa M, Scholey JM, Vale RD, Walczak CE, Wordeman L (October 2004). "A standardized kinesin nomenclature". The Journal of Cell Biology. 167 (1): 19–22. doi:10.1083/jcb.200408113. PMC 2041940. PMID 15479732.

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Kinesin motor domain Provide feedback

No Pfam abstract.

Literature references

  1. Sablin EP, Kull FJ, Cooke R, Vale RD, Fletterick RJ; , Nature 1996;380:550-555.: Crystal-structure of the motor domain af the kinesin-related motor NCD PUBMED:8606780 EPMC:8606780

  2. Kozielski F, Sack S, Marx A, Thormahlen M, Schonbrunn E, Biou V, Thompson A, Mandelkow EM, Mandelkow E; , Cell 1997;91:985-994.: The crystal structure of dimeric kinesin and implications for microtubule-dependent motility. PUBMED:9428521 EPMC:9428521

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001752

Kinesin [ PUBMED:8542443 , PUBMED:2142876 , PUBMED:14732151 ] is a microtubule-associated force-producing protein that may play a role in organelle transport. The kinesin motor activity is directed toward the microtubule's plus end. Kinesin is an oligomeric complex composed of two heavy chains and two light chains. The maintenance of the quaternary structure does not require interchain disulphide bonds.

The heavy chain is composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it is known to hydrolyse ATP, to bind and move on microtubules), a central alpha-helical coiled coil domain that mediates the heavy chain dimerisation; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.

The kinesin motor domain comprises five motifs, namely N1 (P-loop), N2 (Switch I), N3 (Switch II), N4 and L2 (KVD finger) [ PUBMED:20587735 ]. It has a mixed eight stranded beta-sheet core with flanking solvent exposed alpha-helices and a small three-stranded antiparallel beta-sheet in the N-terminal region [ PUBMED:15236970 ].

A number of proteins have been recently found that contain a domain similar to that of the kinesin 'motor' domain [ PUBMED:8542443 , PUBMED:1832505 ]:

  • Drosophila melanogaster claret segregational protein (ncd). Ncd is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The ncd motor activity is directed toward the microtubule's minus end.
  • Homo sapiens CENP-E [ PUBMED:1832505 ]. CENP-E is a protein that associates with kinetochores during chromosome congression, relocates to the spindle midzone at anaphase, and is quantitatively discarded at the end of the cell division. CENP-E is probably an important motor molecule in chromosome movement and/or spindle elongation.
  • H. sapiens mitotic kinesin-like protein-1 (MKLP-1), a motor protein whose activity is directed toward the microtubule's plus end.
  • Saccharomyces cerevisiae KAR3 protein, which is essential for nuclear fusion during mating. KAR3 may mediate microtubule sliding during nuclear fusion and possibly mitosis.
  • S. cerevisiae CIN8 and KIP1 proteins which are required for the assembly of the mitotic spindle. Both proteins seem to interact with spindle microtubules to produce an outwardly directed force acting upon the poles.
  • Emericella nidulans (Aspergillus nidulans) bimC, which plays an important role in nuclear division.
  • A. nidulans klpA.
  • Caenorhabditis elegans unc-104, which may be required for the transport of substances needed for neuronal cell differentiation.
  • C. elegans osm-3.
  • Xenopus laevis Eg5, which may be involved in mitosis.
  • Arabidopsis thaliana KatA, KatB and katC.
  • Chlamydomonas reinhardtii FLA10/KHP1 and KLP1. Both proteins seem to play a role in the rotation or twisting of the microtubules of the flagella.
  • C. elegans hypothetical protein T09A5.2.

The kinesin motor domain is located in the N-terminal part of most of the above proteins, with the exception of KAR3, klpA, and ncd where it is located in the C-terminal section.

The kinesin motor domain contains about 330 amino acids. An ATP-binding motif of type A is found near position 80 to 90, the C-terminal half of the domain is involved in microtubule-binding.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan P-loop_NTPase (CL0023), which has the following description:

AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].

The clan contains the following 245 members:

6PF2K AAA AAA-ATPase_like AAA_10 AAA_11 AAA_12 AAA_13 AAA_14 AAA_15 AAA_16 AAA_17 AAA_18 AAA_19 AAA_2 AAA_21 AAA_22 AAA_23 AAA_24 AAA_25 AAA_26 AAA_27 AAA_28 AAA_29 AAA_3 AAA_30 AAA_31 AAA_32 AAA_33 AAA_34 AAA_35 AAA_5 AAA_6 AAA_7 AAA_8 AAA_9 AAA_PrkA ABC_ATPase ABC_tran ABC_tran_Xtn Adeno_IVa2 Adenylsucc_synt ADK AFG1_ATPase AIG1 APS_kinase Arf ArsA_ATPase ATP-synt_ab ATP_bind_1 ATP_bind_2 ATPase ATPase_2 Bac_DnaA BCA_ABC_TP_C Beta-Casp bpMoxR BrxC_BrxD BrxL_ATPase Cas_Csn2 Cas_St_Csn2 CbiA CBP_BcsQ CDC73_C CENP-M CFTR_R CLP1_P CMS1 CoaE CobA_CobO_BtuR CobU cobW CPT CSM2 CTP_synth_N Cytidylate_kin Cytidylate_kin2 DAP3 DEAD DEAD_2 divDNAB DLIC DNA_pack_C DNA_pack_N DNA_pol3_delta DNA_pol3_delta2 DnaB_C dNK DO-GTPase1 DO-GTPase2 DUF1611 DUF2075 DUF2326 DUF2478 DUF257 DUF2813 DUF3584 DUF463 DUF4914 DUF5906 DUF6079 DUF815 DUF835 DUF87 DUF927 Dynamin_N Dynein_heavy Elong_Iki1 ELP6 ERCC3_RAD25_C Exonuc_V_gamma FeoB_N Fer4_NifH Flavi_DEAD FTHFS FtsK_SpoIIIE G-alpha Gal-3-0_sulfotr GBP GBP_C GpA_ATPase GpA_nuclease GTP_EFTU Gtr1_RagA Guanylate_kin GvpD_P-loop HDA2-3 Helicase_C Helicase_C_2 Helicase_C_4 Helicase_RecD HerA_C Herpes_Helicase Herpes_ori_bp Herpes_TK HydF_dimer HydF_tetramer Hydin_ADK IIGP IPPT IPT iSTAND IstB_IS21 KAP_NTPase KdpD Kinase-PPPase Kinesin KTI12 LAP1_C LpxK MCM MeaB MEDS Mg_chelatase Microtub_bd MipZ MMR_HSR1 MMR_HSR1_C MobB MukB Mur_ligase_M MutS_V Myosin_head NACHT NAT_N NB-ARC NOG1 NTPase_1 NTPase_P4 ORC3_N P-loop_TraG ParA Parvo_NS1 PAXNEB PduV-EutP PhoH PIF1 Ploopntkinase1 Ploopntkinase2 Ploopntkinase3 Podovirus_Gp16 Polyoma_lg_T_C Pox_A32 PPK2 PPV_E1_C PRK PSY3 Rad17 Rad51 Ras RecA ResIII RHD3_GTPase RhoGAP_pG1_pG2 RHSP RNA12 RNA_helicase Roc RsgA_GTPase RuvB_N SbcC_Walker_B SecA_DEAD Senescence Septin Sigma54_activ_2 Sigma54_activat SKI SMC_N SNF2-rel_dom SpoIVA_ATPase Spore_III_AA SRP54 SRPRB SulA Sulfotransfer_1 Sulfotransfer_2 Sulfotransfer_3 Sulfotransfer_4 Sulfotransfer_5 Sulphotransf SWI2_SNF2 T2SSE T4SS-DNA_transf TerL_ATPase Terminase_3 Terminase_6N Thymidylate_kin TIP49 TK TmcA_N TniB Torsin TraG-D_C tRNA_lig_kinase TrwB_AAD_bind TsaE UvrB UvrD-helicase UvrD_C UvrD_C_2 Viral_helicase1 VirC1 VirE YqeC Zeta_toxin Zot


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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: kinesin;
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A , Finn RD
Number in seed: 69
Number in full: 61809
Average length of the domain: 298.50 aa
Average identity of full alignment: 33 %
Average coverage of the sequence by the domain: 30.80 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 29.3 29.3
Trusted cut-off 29.3 29.3
Noise cut-off 29.2 29.2
Model length: 332
Family (HMM) version: 26
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Kinesin domain has been found. There are 356 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A068FIK2 View 3D Structure Click here
A0A0G2K857 View 3D Structure Click here
A0A0G2K8Z9 View 3D Structure Click here
A0A0G2L7N0 View 3D Structure Click here
A0A0P0UX31 View 3D Structure Click here
A0A0P0Y3Q5 View 3D Structure Click here
A0A0R0EWD3 View 3D Structure Click here
A0A0R0F1M3 View 3D Structure Click here
A0A0R0F2G7 View 3D Structure Click here
A0A0R0FBU8 View 3D Structure Click here
A0A0R0FG14 View 3D Structure Click here
A0A0R0FII7 View 3D Structure Click here
A0A0R0FP22 View 3D Structure Click here
A0A0R0FPY2 View 3D Structure Click here
A0A0R0FQ41 View 3D Structure Click here
A0A0R0GKL1 View 3D Structure Click here
A0A0R0HAG1 View 3D Structure Click here
A0A0R0HB65 View 3D Structure Click here
A0A0R0HFC8 View 3D Structure Click here
A0A0R0HRH5 View 3D Structure Click here
A0A0R0I7D7 View 3D Structure Click here
A0A0R0I8J8 View 3D Structure Click here
A0A0R0IC90 View 3D Structure Click here
A0A0R0ICV3 View 3D Structure Click here
A0A0R0IQQ6 View 3D Structure Click here
A0A0R0ITC3 View 3D Structure Click here
A0A0R0J4C3 View 3D Structure Click here
A0A0R0J7C8 View 3D Structure Click here
A0A0R0JQF0 View 3D Structure Click here
A0A0R0JZ28 View 3D Structure Click here
A0A0R0K0F1 View 3D Structure Click here
A0A0R0KJ22 View 3D Structure Click here
A0A0R0KJB3 View 3D Structure Click here
A0A0R0KNM8 View 3D Structure Click here
A0A0R0LD71 View 3D Structure Click here
A0A0R4IGG0 View 3D Structure Click here
A0A0R4IM96 View 3D Structure Click here
A0A0R4IWI7 View 3D Structure Click here
A0A126GUN8 View 3D Structure Click here
A0A1B0GSG7 View 3D Structure Click here