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776  structures 2330  species 0  interactions 93885  sequences 2547  architectures

Family: Kelch_1 (PF01344)

Summary: Kelch motif

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 "Kelch motif". More...

Kelch motif Edit Wikipedia article

Kelch motif
PDB 1gof EBI.jpg
Structure of Galactose oxidase containing kelch repeats.[1]
Identifiers
SymbolKelch_1
PfamPF01344
InterProIPR006652
SMARTKelch
SCOPe1gof / SUPFAM
OPM superfamily319
OPM protein3ii7
Kelch motif
Identifiers
SymbolKelch_2
PfamPF07646
Pfam clanCL0186
InterProIPR011498
SCOPe1gof / SUPFAM
Galactose oxidase, central domain
Identifiers
SymbolKelch_3
PfamPF13415
Pfam clanCL0186
Galactose oxidase, central domain
Identifiers
SymbolKelch_4
PfamPF13418
Pfam clanCL0186
Kelch motif
Identifiers
SymbolKelch_5
PfamPF13854
Pfam clanCL0186
Kelch motif
Identifiers
SymbolKelch_6
PfamPF13964
Pfam clanCL0186

The Kelch motif is a region of protein sequence found widely in proteins from bacteria and eukaryotes.[2] This sequence motif is composed of about 50 amino acid residues which form a structure of a four stranded beta-sheet "blade". This sequence motif is found in between five and eight tandem copies per protein which fold together to form a larger circular solenoid structure called a beta-propeller domain.

Proteins containing Kelch motifs

The Kelch motif is widely found in eukaryotic and bacterial species. Notably the human genome contains around 100 proteins containing the Kelch motif. Within individual proteins the motif occurs multiple times. For example, the motif appears 6 times in Drosophila egg-chamber regulatory protein. The motif is also found in mouse protein MIPP[3] and in a number of poxviruses. In addition, kelch repeats have been recognised in alpha- and beta-scruin,[4][5] in galactose oxidase from the fungus Dactylium dendroides[6][7] and in the Escherichia coli NanM protein, that is a sialic acid mutarotase.[8]

Structure

The structure of galactose oxidase reveals that the repeated Kelch sequence motif corresponds to a 4-stranded anti-parallel beta-sheet motif that forms the repeat unit in a super-barrel structural fold commonly known as a beta propeller.[9]

Function

The known functions of kelch-containing proteins are diverse:

  • scruin is an actin cross-linking protein;
  • galactose oxidase catalyses the oxidation of the hydroxyl group at the C6 position in D-galactose;
  • neuraminidase hydrolyses sialic acid residues from glycoproteins;
  • NanM is a sialic acid mutarotase, involved in efficient utilisation of sialic acid by bacteria;
  • kelch may have a cytoskeletal function, as it is localised to the actin-rich ring canals that connect the 15 nurse cells to the developing oocyte in Drosophila.[4]

See also

References

  1. ^ Ito N, Phillips SE, Stevens C, et al. (March 1991). "Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase". Nature. 350 (6313): 87–90. doi:10.1038/350087a0. PMID 2002850.
  2. ^ Adams J, Kelso R, Cooley L (January 2000). "The kelch repeat superfamily of proteins: propellers of cell function". Trends Cell Biol. 10 (1): 17–24. doi:10.1016/S0962-8924(99)01673-6. PMID 10603472.
  3. ^ Xue F, Cooley L (1993). "kelch encodes a component of intercellular bridges in Drosophila egg chambers". Cell. 72 (5): 681–693. doi:10.1016/0092-8674(93)90397-9. PMID 8453663.
  4. ^ a b Way M, Sanders M, Matsudaira P, Chafel M, Knight A, Tu YH (1995). "beta-Scruin, a homologue of the actin crosslinking protein scruin, is localized to the acrosomal vesicle of Limulus sperm". J. Cell Sci. 108: 3155–3162. PMID 7593276.
  5. ^ Way M, Sakai J, Sanders M, Garcia C, Matsudaira P (1995). "Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm". J. Cell Biol. 128 (1): 51–60. doi:10.1083/jcb.128.1.51. PMC 2120335. PMID 7822422.
  6. ^ Doolittle RF, Bork P (1994). "Drosophila kelch motif is derived from a common enzyme fold". J. Mol. Biol. 236 (5): 1277–1282. doi:10.1016/0022-2836(94)90056-6. PMID 8126718.
  7. ^ Keen JN, Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Yadav KD, Knowles PF (1991). "Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase". Nature. 350 (6313): 87–90. doi:10.1038/350087a0. PMID 2002850.
  8. ^ Severi E, Müller A, Potts JR, Leech A, Williamson D, Wilson KS, Thomas GH (2008). "Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT". J. Biol. Chem. 283 (8): 4841–4849. doi:10.1074/jbc.m707822200. PMID 18063573.
  9. ^ Ito N, Phillips SE, Yadav KD, Knowles PF (1994). "Crystal structure of a free radical enzyme, galactose oxidase". J. Mol. Biol. 238 (5): 794–814. doi:10.1006/jmbi.1994.1335. PMID 8182749.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR006652
This article incorporates text from the public domain Pfam and InterPro: IPR011498

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

This is the Wikipedia entry entitled "Kelch protein". More...

Kelch protein Edit Wikipedia article

Kelch motif
1gof front.GIF
Identifiers
SymbolKelch_1
PfamPF01344
InterProIPR006652
SCOPe1gof / SUPFAM

Kelch proteins (and Kelch-like proteins) are a widespread group of proteins that contain multiple Kelch motifs. The kelch domain generally occurs as a set of five to seven kelch tandem repeats that form a β-propeller tertiary structure. Kelch-repeat β-propellers are generally involved in protein–protein interactions, though the large diversity of domain architectures and limited sequence identity between kelch motifs make characterisation of the kelch superfamily difficult.

Structure

The N-terminus of several Kelch proteins contain other protein domains, including Discoidin, F-box, and Broad-complex, Tramtrack, Bric-a-Brac/Poxvirus and Zincfinger (BTB/POZ) domains. Kelch proteins may also only have a β-propeller architecture. The BTB domain of kelch proteins (if present) allows the formation of homo- or heterodimers that mediate protein–protein interactions.

The C-terminus of Kelch proteins contains kelch repeats. Each kelch repeat is a sequence of 44–55 amino acids in length, usually occurring in clusters of 4 – 7 repeats.

Each kelch repeat forms a "blade" of the β-propeller fold, consisting of a four-stranded antiparallel β-sheet secondary structure, arranged radially around a central axis, packed onto its adjoining repeats via hydrophobic contacts.

Kelch-repeat β-propellers undergo a variety of binding interactions with other proteins, notably the actin filaments of a cell.

Function

Kelch like proteins are known to act as substrate adaptors for Cullin 3 ubiquitin ligases.

Organisms

The first Kelch protein (from which this family derives its name) was isolated from Drosophila, in which Kelch-mutant females lay sterile, cup-shaped eggs;[1] "Kelch" is German for "chalice", or "cup". Kelch proteins have also been isolated in many other animals, plants, bacteria, fungi, and even virus (restricted to Poxviridae).

Human proteins containing Kelch motifs

ATRN; ATRNL1; CCIN; ENC1; FBXO42; GAN; HCFC1; HCFC2; IPP; IVNS1ABP; KBTBD10; KBTBD11; KBTBD2; KBTBD3; KBTBD4; KBTBD5; KBTBD6; KBTBD7; KBTBD8; KEAP1; KIAA1900; KLHDC1; KLHDC2; KLHDC3; KLHDC4; KLHDC5; KLHDC6; KLHDC7A; KLHDC7B; KLHDC8A; KLHDC8B; KLHDC9; KLHDC10; KLHL1; KLHL10; KLHL11; KLHL12; KLHL13; KLHL14; KLHL15; KLHL17; KLHL18; KLHL2; KLHL20; KLHL21; KLHL22; KLHL23; KLHL24; KLHL25; KLHL26; KLHL28; KLHL29; KLHL3; KLHL30; KLHL31; KLHL32; KLHL34; KLHL4; KLHL40; KLHL5; KLHL6; KLHL7; KLHL8; KLHL9; LZTR1; MEGF8; MKLN1; RABEPK; SARCOSIN;

References

  1. ^ UNDERSTANDING THE FUNCTION OF ACTIN-BINDING PROTEINS THROUGH GENETIC ANALYSIS OF DROSOPHILA OOGENESIS, by Andrew M. Hudson and Lynn Cooley; in the Annual Review of Genetics, Vol. 36: 455–488 (Volume publication date December 2002); retrieved 12 December 2013


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.

Kelch motif Provide feedback

The kelch motif was initially discovered in Kelch (Q04652). In this protein there are six copies of the motif. It has been shown that Q04652 is related to Galactose Oxidase [1] for which a structure has been solved [2]. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in PF00064 PF00400 and PF00415.

Literature references

  1. Bork P, Doolittle RF; , J Mol Biol 1994;236:1277-1282.: Drosophila kelch motif is derived from a common enzyme fold. PUBMED:8126718 EPMC:8126718

  2. Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF; , Nature 1991;350:87-90.: Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. PUBMED:2002850 EPMC:2002850

  3. Li X, Zhang D, Hannink M, Beamer LJ; , J Biol Chem 2004;279:54750-54758.: Crystal structure of the Kelch domain of human Keap1. PUBMED:15475350 EPMC:15475350


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006652

Kelch is a 50-residue motif, named after the Drosophila mutant in which it was first identified [ PUBMED:8453663 ]. This sequence motif represents one beta-sheet blade, and several of these repeats can associate to form a beta-propeller. For instance, the motif appears 6 times in Drosophila egg-chamber regulatory protein (also known as ring canal kelch protein), creating a 6-bladed beta-propeller. The motif is also found in mouse protein MIPP [ PUBMED:8453663 ] and in a number of poxviruses. In addition, kelch repeats have been recognised in alpha- and beta-scruin [ PUBMED:7593276 , PUBMED:7822422 ], and in galactose oxidase from the fungus Dactylium dendroides [ PUBMED:8126718 , PUBMED:2002850 ]. The structure of galactose oxidase reveals that the repeated sequence corresponds to a 4-stranded anti-parallel beta-sheet motif that forms the repeat unit in a super-barrel structural fold [ PUBMED:8182749 ].

The known functions of kelch-containing proteins are diverse: scruin is an actin cross-linking protein; galactose oxidase catalyses the oxidation of the hydroxyl group at the C6 position in D-galactose; and kelch may have a cytoskeletal function, as it is localised to the actin-rich ring canals that connect the 15 nurse cells to the developing oocyte in Drosophila [ PUBMED:7593276 ]. Nevertheless, based on the location of the kelch pattern in the catalytic unit in galactose oxidase, functionally important residues have been predicted in glyoxal oxidase [ PUBMED:8126718 ].

This entry represents a type of kelch sequence motif that comprises one beta-sheet blade.

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 Beta_propeller (CL0186), which has the following description:

This large clan contains proteins that contain beta propellers. These are composed of between 6 and 8 repeats. The individual repeats are composed of a four stranded sheet. The clan includes families such as WD40 Pfam:PF00400 where the individual repeats are modeled. The clan also includes families where the entire propeller is modeled such as Pfam:PF02239 usually because the individual repeats are not discernible. These proteins carry out a very wide diversity of functions including catalysis.

The clan contains the following 88 members:

ANAPC4_WD40 APMAP_N Arylesterase Arylsulfotran_2 Arylsulfotrans B_lectin BBS2_Mid Beta_propel Coatomer_WDAD CPSF_A CyRPA Cytochrom_D1 Dpp_8_9_N DPPIV_N DPPIV_rep DUF1513 DUF1668 DUF2415 DUF3748 DUF4221 DUF4933 DUF4934 DUF5046 DUF5050 DUF5122 DUF5128 DUF5711 DUF839 eIF2A FG-GAP FG-GAP_2 FG-GAP_3 Frtz Ge1_WD40 Glu_cyclase_2 Gmad1 GSDH Hyd_WA IKI3 Itfg2 Kelch_1 Kelch_2 Kelch_3 Kelch_4 Kelch_5 Kelch_6 Lactonase Ldl_recept_b LGFP Lgl_C LVIVD Me-amine-dh_H MgpC MRJP Nbas_N Neisseria_PilC NHL nos_propeller nos_propeller_2 Nucleoporin_N Nup160 PALB2_WD40 PD40 Pectate_lyase22 Peptidase_S9_N PHTB1_N Phytase-like PQQ PQQ_2 PQQ_3 RAG2 RCC1 RCC1_2 Reg_prop SBBP SBP56 SdiA-regulated SGL Str_synth TcdB_toxin_midN Tectonin TolB_like VID27 WD40 WD40_2 WD40_3 WD40_4 WD40_like

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
(147)
Full
(93885)
Representative proteomes UniProt
(200787)
RP15
(16444)
RP35
(38477)
RP55
(81391)
RP75
(109191)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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

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  Seed
(147)
Full
(93885)
Representative proteomes UniProt
(200787)
RP15
(16444)
RP35
(38477)
RP55
(81391)
RP75
(109191)
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
(147)
Full
(93885)
Representative proteomes UniProt
(200787)
RP15
(16444)
RP35
(38477)
RP55
(81391)
RP75
(109191)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   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: [1]
Previous IDs: none
Type: Repeat
Sequence Ontology: SO:0001068
Author: Bateman A
Number in seed: 147
Number in full: 93885
Average length of the domain: 45.80 aa
Average identity of full alignment: 26 %
Average coverage of the sequence by the domain: 20.87 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.1 20.0
Trusted cut-off 20.1 20.0
Noise cut-off 20.0 19.9
Model length: 46
Family (HMM) version: 27
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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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 Kelch_1 domain has been found. There are 776 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
A0A096PXD0 View 3D Structure Click here
A0A096PXD0 View 3D Structure Click here
A0A096PXD0 View 3D Structure Click here
A0A096QCE5 View 3D Structure Click here
A0A096QCE5 View 3D Structure Click here
A0A096QN59 View 3D Structure Click here
A0A0G2K427 View 3D Structure Click here
A0A0G2K427 View 3D Structure Click here
A0A0G2K427 View 3D Structure Click here
A0A0G2K427 View 3D Structure Click here
A0A0G2K427 View 3D Structure Click here
A0A0G2K427 View 3D Structure Click here
A0A0G2K982 View 3D Structure Click here
A0A0G2K982 View 3D Structure Click here
A0A0G2KCC7 View 3D Structure Click here
A0A0G2KCC7 View 3D Structure Click here
A0A0G2KCH4 View 3D Structure Click here
A0A0G2KCH4 View 3D Structure Click here
A0A0G2KCH4 View 3D Structure Click here
A0A0G2KCH4 View 3D Structure Click here
A0A0N4STP4 View 3D Structure Click here
A0A0N4STP4 View 3D Structure Click here
A0A0N4STP4 View 3D Structure Click here
A0A0N7KFI1 View 3D Structure Click here
A0A0P0VGE5 View 3D Structure Click here
A0A0P0VGE5 View 3D Structure Click here
A0A0P0VZH9 View 3D Structure Click here
A0A0P0WES8 View 3D Structure Click here
A0A0P0WES8 View 3D Structure Click here
A0A0P0WIM6 View 3D Structure Click here
A0A0P0WIM6 View 3D Structure Click here
A0A0P0WIM6 View 3D Structure Click here
A0A0P0WIM6 View 3D Structure Click here
A0A0P0WIM6 View 3D Structure Click here
A0A0P0X770 View 3D Structure Click here
A0A0R0EPV2 View 3D Structure Click here
A0A0R0EPV2 View 3D Structure Click here
A0A0R0F2E0 View 3D Structure Click here
A0A0R0F2E0 View 3D Structure Click here
A0A0R0FB22 View 3D Structure Click here
A0A0R0FB22 View 3D Structure Click here
A0A0R0FB22 View 3D Structure Click here
A0A0R0FB22 View 3D Structure Click here
A0A0R0G3L9 View 3D Structure Click here
A0A0R0G3L9 View 3D Structure Click here
A0A0R0G990 View 3D Structure Click here
A0A0R0HHF6 View 3D Structure Click here
A0A0R0HHF6 View 3D Structure Click here
A0A0R0J130 View 3D Structure Click here
A0A0R0J130 View 3D Structure Click here
A0A0R0KDD4 View 3D Structure Click here
A0A0R0KHK4 View 3D Structure Click here
A0A0R0KHK4 View 3D Structure Click here
A0A0R0KK34 View 3D Structure Click here
A0A0R0KK34 View 3D Structure Click here
A0A0R0KTS6 View 3D Structure Click here
A0A0R0KTS6 View 3D Structure Click here
A0A0R0KYZ2 View 3D Structure Click here
A0A0R0KYZ2 View 3D Structure Click here
A0A0R4IAE5 View 3D Structure Click here
A0A0R4IAE5 View 3D Structure Click here
A0A140LFU3 View 3D Structure Click here
A0A140LFU3 View 3D Structure Click here
A0A140LGF5 View 3D Structure Click here
A0A140LGF5 View 3D Structure Click here
A0A140LGQ1 View 3D Structure Click here
A0A140LGQ1 View 3D Structure Click here
A0A140LGQ1 View 3D Structure Click here
A0A140LGQ1 View 3D Structure Click here
A0A140LGQ1 View 3D Structure Click here
A0A140LGZ3 View 3D Structure Click here
A0A140LGZ3 View 3D Structure Click here
A0A140LGZ3 View 3D Structure Click here
A0A1D6DZ84 View 3D Structure Click here
A0A1D6DZ84 View 3D Structure Click here
A0A1D6F561 View 3D Structure Click here
A0A1D6F755 View 3D Structure Click here
A0A1D6FEN3 View 3D Structure Click here
A0A1D6FEN3 View 3D Structure Click here
A0A1D6FEN3 View 3D Structure Click here
A0A1D6GDQ0 View 3D Structure Click here
A0A1D6GSB0 View 3D Structure Click here
A0A1D6GSB0 View 3D Structure Click here
A0A1D6H393 View 3D Structure Click here
A0A1D6H393 View 3D Structure Click here
A0A1D6HNQ0 View 3D Structure Click here
A0A1D6HW85 View 3D Structure Click here
A0A1D6I0M2 View 3D Structure Click here
A0A1D6IAQ7 View 3D Structure Click here
A0A1D6ICZ6 View 3D Structure Click here
A0A1D6LAM6 View 3D Structure Click here
A0A1D6LYG2 View 3D Structure Click here
A0A1D6LYG2 View 3D Structure Click here
A0A1D6LYG2 View 3D Structure Click here
A0A1D6LYG2 View 3D Structure Click here
A0A1D6LYG9 View 3D Structure Click here
A0A1D6LYG9 View 3D Structure Click here
A0A1D6LYG9 View 3D Structure Click here
A0A1D6LYG9 View 3D Structure Click here
A0A1D6MXM9 View 3D Structure Click here
A0A1D6NQ28 View 3D Structure Click here
A0A1D6NQ28 View 3D Structure Click here
A0A1D6NQ28 View 3D Structure Click here
A0A1D6NQ28 View 3D Structure Click here
A0A1D6P2L3 View 3D Structure Click here
A0A1D6PWM4 View 3D Structure Click here
A0A1D6Q3E6 View 3D Structure Click here
A0A1D6Q3E6 View 3D Structure Click here
A0A1D6QAL1 View 3D Structure Click here
A0A1D6QHB9 View 3D Structure Click here
A0A286YC09 View 3D Structure Click here
A0A286YD60 View 3D Structure Click here
A0A286YD60 View 3D Structure Click here
A0A2I3BRZ3 View 3D Structure Click here
A0A2I3BRZ3 View 3D Structure Click here
A0A2I3BRZ3 View 3D Structure Click here
A0A2R8PXW6 View 3D Structure Click here
A0A2R8PXW6 View 3D Structure Click here
A0A2R8PXW6 View 3D Structure Click here
A0A2R8PXW6 View 3D Structure Click here
A0A2R8PXW6 View 3D Structure Click here
A0A2R8Q0Z4 View 3D Structure Click here
A0A2R8Q0Z4 View 3D Structure Click here
A0A2R8Q0Z4 View 3D Structure Click here
A0A2R8Q0Z4 View 3D Structure Click here
A0A2R8Q0Z4 View 3D Structure Click here
A0A2R8Q0Z4 View 3D Structure Click here
A0A2R8Q1W5 View 3D Structure Click here
A0A2R8Q1W5 View 3D Structure Click here
A0A2R8Q1W5 View 3D Structure Click here
A0A2R8Q1W5 View 3D Structure Click here
A0A2R8Q1W5 View 3D Structure Click here
A0A2R8Q4M5 View 3D Structure Click here
A0A2R8Q4M5 View 3D Structure Click here
A0A2R8Q5T3 View 3D Structure Click here
A0A2R8Q5T3 View 3D Structure Click here
A0A2R8Q5T3 View 3D Structure Click here
A0A2R8Q5T3 View 3D Structure Click here
A0A2R8Q5T3 View 3D Structure Click here
A0A2R8Q5T3 View 3D Structure Click here
A0A2R8Q616 View 3D Structure Click here
A0A2R8Q616 View 3D Structure Click here
A0A2R8Q616 View 3D Structure Click here
A0A2R8Q616 View 3D Structure Click here
A0A2R8Q616 View 3D Structure Click here
A0A2R8Q662 View 3D Structure Click here
A0A2R8Q6R0 View 3D Structure Click here
A0A2R8Q6R0 View 3D Structure Click here
A0A2R8Q6R0 View 3D Structure Click here
A0A2R8Q6R0 View 3D Structure Click here
A0A2R8Q6R0 View 3D Structure Click here
A0A2R8Q9E7 View 3D Structure Click here
A0A2R8Q9E7 View 3D Structure Click here
A0A2R8Q9E7 View 3D Structure Click here
A0A2R8Q9E7 View 3D Structure Click here
A0A2R8Q9E7 View 3D Structure Click here
A0A2R8QC39 View 3D Structure Click here
A0A2R8QCY5 View 3D Structure Click here
A0A2R8QCY5 View 3D Structure Click here
A0A2R8QCY5 View 3D Structure Click here
A0A2R8QCY5 View 3D Structure Click here
A0A2R8QCY5 View 3D Structure Click here
A0A2R8QD64 View 3D Structure Click here
A0A2R8QD64 View 3D Structure Click here
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