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1040  structures 5208  species 0  interactions 451226  sequences 14014  architectures

Family: Ank_2 (PF12796)

Summary: Ankyrin repeats (3 copies)

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Ankyrin repeat". More...

Ankyrin repeat Edit Wikipedia article

Ankyrin repeat domain
Ankyrin R membrane-binding domain 1N11.png
Ribbon diagram of a fragment of the membrane-binding domain of ankyrin R.[1]
Identifiers
SymbolAnk
PfamPF00023
InterProIPR002110
SMARTSM00248
PROSITEPDOC50088
SCOPe1awc / SUPFAM

The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops, first discovered in signaling proteins in yeast Cdc10 and Drosophila Notch. Domains consisting of ankyrin tandem repeats mediate protein–protein interactions and are among the most common structural motifs in known proteins. They appear in bacterial, archaeal, and eukaryotic proteins, but are far more common in eukaryotes. Ankyrin repeat proteins, though absent in most viruses, are common among poxviruses. Most proteins that contain the motif have four to six repeats, although its namesake ankyrin contains 24, and the largest known number of repeats is 34, predicted in a protein expressed by Giardia lamblia.[2]

Ankyrin repeats typically fold together to form a single, linear solenoid structure called ankyrin repeat domains. These domains are one of the most common protein–protein interaction platforms in nature. They occur in a large number of functionally diverse proteins, mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers.[3] The repeat has been found in proteins of diverse function such as transcriptional initiators, cell cycle regulators, cytoskeletal, ion transporters, and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function, since there is no specific sequence or structure that is universally recognised by it.

Considering the atomic structures of individual ankyrin repeats, the loop is often a type 1 beta bulge loop, while both alpha-helices commonly have a Schellman loop at their N-terminus.

Role in protein folding

The ankyrin-repeat sequence motif has been studied using multiple sequence alignment to determine conserved amino acid residues critical for folding and stability. The residues on the wide lateral surface of ankyrin repeat structures are variable, often hydrophobic, and involved mainly in mediating protein–protein interactions. An artificial protein design based on a consensus sequence derived from sequence alignment has been synthesized and found to fold stably, representing the first designed protein with multiple repeats.[4] More extensive design strategies have used combinatorial sequences to "evolve" ankyrin-repeats that recognize particular protein targets, a technique that has been presented as an alternative to antibody design for applications requiring high-affinity binding.[5] A structure-based study involving a range of ankyrin proteins of known structures, shows that consensus-based ankyrin proteins are very stable since they maximize the energetic gap between the folding and unfolding structures, encoding a densely connected network of favourable interactions among conserved sequence motifs, like the TPLX motif.[6] The same study shows that insertions in the canonical framework of ankyrin repeats are enriched in conflictive interactions, that are related to function. The same applies to interactions surrounding deletion hotspots. These might be related to complex folding/unfolding transitions that are important to the partner recognition and interaction.

Ankyrin-repeat proteins present an unusual problem in the study of protein folding, which has largely focused on globular proteins that form well-defined tertiary structure stabilized by long-range, nonlocal residue-residue contacts. Ankyrin repeats, by contrast, contain very few such contacts (that is, they have a low contact order). Most studies have found that ankyrin repeats fold in a two-state folding mechanism, suggesting a high degree of folding cooperativity despite the local inter-residue contacts and the evident need for successful folding with varying numbers of repeats. Some evidence, based on synthesis of truncated versions of natural repeat proteins,[7] and on the examination of phi values,[8] suggests that the C-terminus forms the folding nucleation site.

Clinical significance

Ankyrin-repeat proteins have been associated with a number of human diseases. These proteins include the cell cycle inhibitor p16, which is associated with cancer, and the Notch protein (a key component of cell signalling pathways) which can cause the neurological disorder CADASIL when the repeat domain is disrupted by mutations.[2]

A specialized family of ankyrin proteins known as muscle ankyrin repeat proteins (MARPs) are involved with the repair and regeneration of muscle tissue following damage due to injury and stress.[9]

A natural variation between glutamine and lysine at position 703 in the 11th ankyrin repeat of ANKK1, known as the TaqI A1 allele,[10] has been credited with encouraging addictive behaviours such as obesity, alcoholism, nicotine dependency and the Eros love style[citation needed] while discouraging juvenile delinquency and neuroticism-anxiety.[11][failed verification] The variation may affect the specificity of protein interactions made by the ANKK1 protein kinase through this repeat[citation needed].

Human proteins containing this repeat

ABTB1; ABTB2; ACBD6; ACTBL1; ANK1; ANK2; ANK3; ANKAR; ANKDD1A; ANKEF1; ANKFY1; ANKHD1; ANKIB1; ANKK1; ANKMY1; ANKMY2; ANKRA2; ANKRD1; ANKRD10; ANKRD11; ANKRD12; ANKRD13; ANKRD13A; ANKRD13B; ANKRD13C; ANKRD13D; ANKRD15; ANKRD16; ANKRD17; ANKRD18A; ANKRD18B; ANKRD19; ANKRD2; ANKRD20A1; ANKRD20A2; ANKRD20A3; ANKRD20A4; ANKRD21; ANKRD22; ANKRD23; ANKRD24; ANKRD25; ANKRD26; ANKRD27; ANKRD28; ANKRD30A; ANKRD30B; ANKRD30BL; ANKRD32; ANKRD33; ANKRD35; ANKRD36; ANKRD36B; ANKRD37; ANKRD38; ANKRD39; ANKRD40; ANKRD41; ANKRD42; ANKRD43; ANKRD44; ANKRD45; ANKRD46; ANKRD47; ANKRD49 [uk]; ANKRD50; ANKRD52; ANKRD53; ANKRD54; ANKRD55; ANKRD56; ANKRD57; ANKRD58; ANKRD60; ANKRD6; ANKRD7; ANKRD9; ANKS1A; ANKS3; ANKS4B; ANKS6; ANKZF1; ASB1; ASB10; ASB11; ASB12; ASB13; ASB14; ASB15; ASB16; ASB2; ASB3; ASB4; ASB5; ASB6; ASB7; ASB8; ASB9; ASZ1; BARD1; BAT4; BAT8; BCL3; BCOR; BCORL1; BTBD11; CAMTA1; CAMTA2; CASKIN1; CASKIN2; CCM1; CDKN2A; CDKN2B; CDKN2C; CDKN2D; CENTB1; CENTB2; CENTB5; CENTG1; CENTG2; CENTG3; CLIP3; CLIP4; CLPB; CTGLF1; CTGLF2; CTGLF3; CTGLF4; CTGLF5; CTTNBP2; DAPK1; DDEF1; DDEF2; DDEFL1; DGKI; DGKZ; DP58; DYSFIP1; DZANK; EHMT1; EHMT2; ESPN; FANK1; FEM1A; FEM1B; GABPB2; GIT1; GIT2; GLS; GLS2; HACE1; HECTD1; IBTK; ILK; INVS; KIDINS220; KRIT1; LRRK1; MAIL; MIB1; MIB2; MPHOSPH8; MTPN; MYO16; NFKB1; NFKB2; NFKBIA; NFKBIB; NFKBIE; NFKBIL1; NFKBIL2; NOTCH1; NOTCH2; NOTCH3; NOTCH4; NRARP; NUDT12; OSBPL1A; OSTF1; PLA2G6; POTE14; POTE15; POTE8; PPP1R12A; PPP1R12B; PPP1R12C; PPP1R13B; PPP1R13L; PPP1R16A; PPP1R16B; PSMD10; RAI14; RFXANK; RIPK4; RNASEL; SHANK1; SHANK2; SHANK3; SNCAIP; TA-NFKBH; TEX14; TNKS; TNKS2; TNNI3K; TP53BP2; TRP7; TRPA1; TRPC3; TRPC4; TRPC5; TRPC6; TRPC7; TRPV1; TRPV2; TRPV3; TRPV4; TRPV5; TRPV6; UACA; USH1G; ZDHHC13; ZDHHC17;

See also

  • DARPin (designed ankyrin repeat protein), an engineered antibody mimetic based on the structure of ankyrin repeats

References

  1. ^ PDB: 1N11​; Michaely P, Tomchick DR, Machius M, Anderson RG (December 2002). "Crystal structure of a 12 ANK repeat stack from human ANK1". EMBO J. 21 (23): 6387–96. doi:10.1093/emboj/cdf651. PMC 136955. PMID 12456646.
  2. ^ a b Mosavi L, Cammett T, Desrosiers D, Peng Z (2004). "The ankyrin repeat as molecular architecture for protein recognition". Protein Sci. 13 (6): 1435–48. doi:10.1110/ps.03554604. PMC 2279977. PMID 15152081. Archived from the original on 2004-09-07.
  3. ^ Bork P (December 1993). "Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?". Proteins. 17 (4): 363–74. doi:10.1002/prot.340170405. PMID 8108379.
  4. ^ Mosavi LK, Minor DL, Peng ZY (Dec 2002). "Consensus-derived structural determinants of the ankyrin repeat motif". Proc Natl Acad Sci USA. 99 (25): 16029–34. Bibcode:2002PNAS...9916029M. doi:10.1073/pnas.252537899. PMC 138559. PMID 12461176.
  5. ^ Binz HK, Amstutz P, Kohl A, et al. (May 2004). "High-affinity binders selected from designed ankyrin repeat protein libraries". Nat. Biotechnol. 22 (5): 575–82. doi:10.1038/nbt962. PMID 15097997.
  6. ^ Parra RG, Espada R, Verstraete N, Ferreiro DU, et al. (Dec 2015). "Structural and Energetic Characterization of the Ankyrin Repeat Protein Family". PLoS Comput. Biol. 12 (11): 575–82. Bibcode:2015PLSCB..11E4659P. doi:10.1371/journal.pcbi.1004659. PMC 4687027. PMID 26691182.
  7. ^ Zhang B, Peng Z (Jun 2000). "A minimum folding unit in the ankyrin repeat protein p16(INK4)". J Mol Biol. 299 (4): 1121–32. doi:10.1006/jmbi.2000.3803. PMID 10843863.
  8. ^ Tang KS, Fersht AR, Itzhaki LS (Jan 2003). "Sequential unfolding of ankyrin repeats in tumor suppressor p16". Structure. 11 (1): 67–73. doi:10.1016/S0969-2126(02)00929-2. PMID 12517341.
  9. ^ Miller MK, Bang ML, Witt CC, et al. (Nov 2003). "The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules". J Mol Biol. 333 (5): 951–64. doi:10.1016/j.jmb.2003.09.012. PMID 14583192.
  10. ^ Neville MJ, Johnstone EC, Walton RT (Jun 2004). "Identification and characterization of ANKK1: a novel kinase gene closely linked to DRD2 on chromosome band 11q23.1". Hum. Mutat. 23 (6): 540–5. doi:10.1002/humu.20039. PMID 15146457.
  11. ^ "NCBI Gene summary for DRD2". (interim reference)

External links

This article incorporates text from the public domain Pfam and InterPro: IPR002110

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.

Ankyrin repeats (3 copies) Provide feedback

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Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR020683

This entry represents the ankyrin repeat-containing domain. These domains contain multiple repeats of a beta(2)-alpha(2) motif. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers [ PUBMED:8108379 ]. The repeat has been found in proteins of diverse function such as transcriptional initiators, cell-cycle regulators, cytoskeletal, ion transporters and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it.

The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [ PUBMED:8875926 , PUBMED:9353127 , PUBMED:9461436 , PUBMED:9865693 ]. Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 o angle. The repeats stack together to form an L-shaped structure [ PUBMED:8875926 , PUBMED:12461176 ].

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 Ank (CL0465), which has the following description:

The ankyrin repeat is a short sequence region that is about 30-34 amino-acids in length. Multiple copies of the repeat composed of two beta strands and two alpha helices combine to form long arrays. In general these repeats are involved in protein-protein interactions. This superfamily also includes some families that are arrays of several repeats.

The clan contains the following 8 members:

Ank Ank_2 Ank_3 Ank_4 Ank_5 AnkUBD DUF3420 DUF3447

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(193)
Full
(451226)
Representative proteomes UniProt
(940172)
RP15
(98727)
RP35
(202511)
RP55
(379680)
RP75
(522420)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

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  Seed
(193)
Full
(451226)
Representative proteomes UniProt
(940172)
RP15
(98727)
RP35
(202511)
RP55
(379680)
RP75
(522420)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(193)
Full
(451226)
Representative proteomes UniProt
(940172)
RP15
(98727)
RP35
(202511)
RP55
(379680)
RP75
(522420)
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Gzipped Download     Download   Download        

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

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: Jackhmmer:Q183I8_CLOD6
Previous IDs: none
Type: Repeat
Sequence Ontology: SO:0001068
Author: Bateman A
Number in seed: 193
Number in full: 451226
Average length of the domain: 87.20 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 30.34 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.3 27.3
Trusted cut-off 27.3 27.3
Noise cut-off 27.2 27.2
Model length: 83
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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Viroids Viroids Unclassified sequence Unclassified sequence

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Structures

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 Ank_2 domain has been found. There are 1040 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
A0A060CZD5 View 3D Structure Click here
A0A061AD72 View 3D Structure Click here
A0A061AD72 View 3D Structure Click here
A0A061AD72 View 3D Structure Click here
A0A061AD72 View 3D Structure Click here
A0A096Q0D7 View 3D Structure Click here
A0A096Q0D7 View 3D Structure Click here
A0A0A6YYL3 View 3D Structure Click here
A0A0A6YYL3 View 3D Structure Click here
A0A0A6YYL3 View 3D Structure Click here
A0A0B4KHT3 View 3D Structure Click here
A0A0G2JT24 View 3D Structure Click here
A0A0G2JT24 View 3D Structure Click here
A0A0G2JT24 View 3D Structure Click here
A0A0G2JT24 View 3D Structure Click here
A0A0G2JT24 View 3D Structure Click here
A0A0G2JVS9 View 3D Structure Click here
A0A0G2JVS9 View 3D Structure Click here
A0A0G2JVS9 View 3D Structure Click here
A0A0G2JVS9 View 3D Structure Click here
A0A0G2JVS9 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JVW3 View 3D Structure Click here
A0A0G2JZ15 View 3D Structure Click here
A0A0G2JZY9 View 3D Structure Click here
A0A0G2JZY9 View 3D Structure Click here
A0A0G2JZY9 View 3D Structure Click here
A0A0G2K149 View 3D Structure Click here
A0A0G2K2D4 View 3D Structure Click here
A0A0G2K3T9 View 3D Structure Click here
A0A0G2K3T9 View 3D Structure Click here
A0A0G2K4R1 View 3D Structure Click here
A0A0G2K4R1 View 3D Structure Click here
A0A0G2K5B7 View 3D Structure Click here
A0A0G2K5V8 View 3D Structure Click here
A0A0G2K5V8 View 3D Structure Click here
A0A0G2K5V8 View 3D Structure Click here
A0A0G2K5V8 View 3D Structure Click here
A0A0G2K6U7 View 3D Structure Click here
A0A0G2K6U7 View 3D Structure Click here
A0A0G2K6W3 View 3D Structure Click here
A0A0G2K808 View 3D Structure Click here
A0A0G2K808 View 3D Structure Click here
A0A0G2K847 View 3D Structure Click here
A0A0G2K889 View 3D Structure Click here
A0A0G2K889 View 3D Structure Click here
A0A0G2K889 View 3D Structure Click here
A0A0G2K8N6 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2K916 View 3D Structure Click here
A0A0G2KA76 View 3D Structure Click here
A0A0G2KA76 View 3D Structure Click here
A0A0G2KB61 View 3D Structure Click here
A0A0G2KK82 View 3D Structure Click here
A0A0G2KK82 View 3D Structure Click here
A0A0G2KK82 View 3D Structure Click here
A0A0G2KK82 View 3D Structure Click here
A0A0G2KME3 View 3D Structure Click here
A0A0G2KME3 View 3D Structure Click here
A0A0G2KME3 View 3D Structure Click here
A0A0G2KME3 View 3D Structure Click here
A0A0G2KWQ6 View 3D Structure Click here
A0A0G2KXP0 View 3D Structure Click here
A0A0G2KXP0 View 3D Structure Click here
A0A0G2KXP0 View 3D Structure Click here
A0A0G2KXP0 View 3D Structure Click here
A0A0K3AV89 View 3D Structure Click here
A0A0K3AV89 View 3D Structure Click here
A0A0K3AV89 View 3D Structure Click here
A0A0K3AV89 View 3D Structure Click here
A0A0K3AV89 View 3D Structure Click here
A0A0M3HEL3 View 3D Structure Click here
A0A0N7KFB4 View 3D Structure Click here
A0A0N7KFB4 View 3D Structure Click here
A0A0N7KFB4 View 3D Structure Click here
A0A0N7KHT9 View 3D Structure Click here
A0A0N7KHT9 View 3D Structure Click here
A0A0N7KHU0 View 3D Structure Click here
A0A0N7KHU0 View 3D Structure Click here
A0A0N7KHU0 View 3D Structure Click here
A0A0N7KLU3 View 3D Structure Click here
A0A0N7KNK3 View 3D Structure Click here
A0A0N7KNK3 View 3D Structure Click here
A0A0N7KPN3 View 3D Structure Click here
A0A0N7KPN3 View 3D Structure Click here
A0A0N7KSJ1 View 3D Structure Click here
A0A0N7KSJ1 View 3D Structure Click here
A0A0N7KSJ1 View 3D Structure Click here
A0A0N7KSJ1 View 3D Structure Click here
A0A0N7KUA3 View 3D Structure Click here
A0A0P0UZ90 View 3D Structure Click here
A0A0P0UZ90 View 3D Structure Click here
A0A0P0UZ90 View 3D Structure Click here
A0A0P0UZD9 View 3D Structure Click here
A0A0P0UZD9 View 3D Structure Click here
A0A0P0VJ73 View 3D Structure Click here
A0A0P0VJ73 View 3D Structure Click here
A0A0P0VJ73 View 3D Structure Click here
A0A0P0VJ86 View 3D Structure Click here
A0A0P0VJ86 View 3D Structure Click here
A0A0P0VPB6 View 3D Structure Click here
A0A0P0VWZ7 View 3D Structure Click here
A0A0P0W1A9 View 3D Structure Click here
A0A0P0W1A9 View 3D Structure Click here
A0A0P0W1A9 View 3D Structure Click here
A0A0P0W1A9 View 3D Structure Click here
A0A0P0W1F9 View 3D Structure Click here
A0A0P0W207 View 3D Structure Click here
A0A0P0W207 View 3D Structure Click here
A0A0P0W207 View 3D Structure Click here
A0A0P0W217 View 3D Structure Click here
A0A0P0W8Z7 View 3D Structure Click here
A0A0P0WMP0 View 3D Structure Click here
A0A0P0WMP0 View 3D Structure Click here
A0A0P0X372 View 3D Structure Click here
A0A0P0X372 View 3D Structure Click here
A0A0P0X5X9 View 3D Structure Click here
A0A0P0X6A0 View 3D Structure Click here
A0A0P0XJZ6 View 3D Structure Click here
A0A0P0XJZ6 View 3D Structure Click here
A0A0P0XK79 View 3D Structure Click here
A0A0P0XK95 View 3D Structure Click here
A0A0P0XK95 View 3D Structure Click here
A0A0P0XKR2 View 3D Structure Click here
A0A0P0XKR2 View 3D Structure Click here
A0A0P0XL59 View 3D Structure Click here
A0A0P0XL82 View 3D Structure Click here
A0A0P0XL82 View 3D Structure Click here
A0A0P0XLJ7 View 3D Structure Click here
A0A0P0XLJ7 View 3D Structure Click here
A0A0P0XLJ7 View 3D Structure Click here
A0A0P0XLJ7 View 3D Structure Click here
A0A0P0XLS8 View 3D Structure Click here
A0A0P0XLX5 View 3D Structure Click here
A0A0P0XZD1 View 3D Structure Click here
A0A0P0XZD1 View 3D Structure Click here
A0A0P0XZL8 View 3D Structure Click here
A0A0P0XZL8 View 3D Structure Click here
A0A0P0XZN9 View 3D Structure Click here
A0A0P0Y0C4 View 3D Structure Click here
A0A0P0Y0M4 View 3D Structure Click here
A0A0P0Y0M4 View 3D Structure Click here
A0A0P0Y0M4 View 3D Structure Click here
A0A0P0Y193 View 3D Structure Click here
A0A0P0Y193 View 3D Structure Click here
A0A0P0Y193 View 3D Structure Click here
A0A0P0Y1Q8 View 3D Structure Click here
A0A0P0Y1Q8 View 3D Structure Click here
A0A0P0Y1Q8 View 3D Structure Click here
A0A0P0Y1Q8 View 3D Structure Click here
A0A0P0Y1Q8 View 3D Structure Click here
A0A0P0Y1Q8 View 3D Structure Click here
A0A0P0Y207 View 3D Structure Click here
A0A0P0Y207 View 3D Structure Click here
A0A0P0Y207 View 3D Structure Click here
A0A0P0Y207 View 3D Structure Click here
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