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89  structures 226  species 0  interactions 49641  sequences 2871  architectures

Family: LRRNT_2 (PF08263)

Summary: Leucine rich repeat N-terminal domain

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 "Leucine-rich repeat". More...

Leucine-rich repeat Edit Wikipedia article

2bnh topview.png
An example of a leucine-rich repeat protein, a porcine ribonuclease inhibitor
Identifiers
SymbolLRR_1
PfamPF00560
Pfam clanCL0022
InterProIPR001611
SCOPe2bnh / SUPFAM
Membranome605
Leucine rich repeat variant
PDB 1lrv EBI.jpg
a leucine-rich repeat variant with a novel repetitive protein structural motif
Identifiers
SymbolLRV
PfamPF01816
Pfam clanCL0020
InterProIPR004830
SCOPe1lrv / SUPFAM
Membranome737
LRR adjacent
PDB 1h6u EBI.jpg
internalin h: crystal structure of fused n-terminal domains.
Identifiers
SymbolLRR_adjacent
PfamPF08191
InterProIPR012569
Membranome341
Leucine rich repeat N-terminal domain
PDB 1xec EBI.jpg
dimeric bovine tissue-extracted decorin, crystal form 2
Identifiers
SymbolLRRNT
PfamPF01462
InterProIPR000372
SMARTLRRNT
SCOPe1m10 / SUPFAM
Membranome127
Leucine rich repeat N-terminal domain
PDB 1ogq EBI.jpg
the crystal structure of pgip (polygalacturonase inhibiting protein), a leucine rich repeat protein involved in plant defense
Identifiers
SymbolLRRNT_2
PfamPF08263
InterProIPR013210
SMARTLRRNT
SCOPe1m10 / SUPFAM
Leucine rich repeat C-terminal domain
PDB 1w8a EBI.jpg
third lrr domain of drosophila slit
Identifiers
SymbolLRRCT
PfamPF01463
InterProIPR000483
SMARTLRRCT
SCOPe1m10 / SUPFAM
LRV protein FeS4 cluster
PDB 1lrv EBI.jpg
a leucine-rich repeat variant with a novel repetitive protein structural motif
Identifiers
SymbolLRV_FeS
PfamPF05484
Pfam clanCL0020
InterProIPR008665
SCOPe1lrv / SUPFAM

A leucine-rich repeat (LRR) is a protein structural motif that forms an α/β horseshoe fold.[1][2] It is composed of repeating 20–30 amino acid stretches that are unusually rich in the hydrophobic amino acid leucine. These tandem repeats commonly fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Typically, each repeat unit has beta strand-turn-alpha helix structure, and the assembled domain, composed of many such repeats, has a horseshoe shape with an interior parallel beta sheet and an exterior array of helices. One face of the beta sheet and one side of the helix array are exposed to solvent and are therefore dominated by hydrophilic residues. The region between the helices and sheets is the protein's hydrophobic core and is tightly sterically packed with leucine residues.

Leucine-rich repeats are frequently involved in the formation of protein–protein interactions.[3][4]

Examples

Leucine-rich repeat motifs have been identified in a large number of functionally unrelated proteins.[5] The best-known example is the ribonuclease inhibitor, but other proteins such as the tropomyosin regulator tropomodulin and the toll-like receptor also share the motif. In fact, the toll-like receptor possesses 10 successive LRR motifs which serve to bind pathogen- and danger-associated molecular patterns.

Although the canonical LRR protein contains approximately one helix for every beta strand, variants that form beta-alpha superhelix folds sometimes have long loops rather than helices linking successive beta strands.

One leucine-rich repeat variant domain (LRV) has a novel repetitive structural motif consisting of alternating alpha- and 310-helices arranged in a right-handed superhelix, with the absence of the beta-sheets present in other leucine-rich repeats.[6]

Associated domains

Leucine-rich repeats are often flanked by N-terminal and C-terminal cysteine-rich domains, but not always as is the case with C5orf36

They also co-occur with LRR adjacent domains. These are small, all beta strand domains, which have been structurally described for the protein Internalin (InlA) and related proteins InlB, InlE, InlH from the pathogenic bacterium Listeria monocytogenes. Their function appears to be mainly structural: They are fused to the C-terminal end of leucine-rich repeats, significantly stabilising the LRR, and forming a common rigid entity with the LRR. They are themselves not involved in protein-protein-interactions but help to present the adjacent LRR-domain for this purpose. These domains belong to the family of Ig-like domains in that they consist of two sandwiched beta sheets that follow the classical connectivity of Ig-domains. The beta strands in one of the sheets is, however, much smaller than in most standard Ig-like domains, making it somewhat of an outlier.[7][8][9]

An iron sulphur cluster is found at the N-terminus of some proteins containing the leucine-rich repeat variant domain (LRV). These proteins have a two-domain structure, composed of a small N-terminal domain containing a cluster of four Cysteine residues that houses the 4Fe:4S cluster, and a larger C-terminal domain containing the LRV repeats.[6] Biochemical studies revealed that the 4Fe:4S cluster is sensitive to oxygen, but does not appear to have reversible redox activity.

See also

References

  1. ^ Kobe B, Deisenhofer J (October 1994). "The leucine-rich repeat: a versatile binding motif". Trends Biochem. Sci. 19 (10): 415–21. doi:10.1016/0968-0004(94)90090-6. PMID 7817399.
  2. ^ Enkhbayar P, Kamiya M, Osaki M, Matsumoto T, Matsushima N (February 2004). "Structural principles of leucine-rich repeat (LRR) proteins". Proteins. 54 (3): 394–403. doi:10.1002/prot.10605. PMID 14747988.
  3. ^ Kobe B, Kajava AV (December 2001). "The leucine-rich repeat as a protein recognition motif". Curr. Opin. Struct. Biol. 11 (6): 725–32. doi:10.1016/S0959-440X(01)00266-4. PMID 11751054.
  4. ^ Gay NJ, Packman LC, Weldon MA, Barna JC (October 1991). "A leucine-rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a beta-sheet structure". FEBS Lett. 291 (1): 87–91. doi:10.1016/0014-5793(91)81110-T. PMID 1657640.
  5. ^ Rothberg JM, Jacobs JR, Goodman CS, Artavanis-Tsakonas S (December 1990). "slit: an extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains". Genes Dev. 4 (12A): 2169–87. doi:10.1101/gad.4.12a.2169. PMID 2176636.
  6. ^ a b Peters JW, Stowell MH, Rees DC (December 1996). "A leucine-rich repeat variant with a novel repetitive protein structural motif". Nat. Struct. Biol. 3 (12): 991–4. doi:10.1038/nsb1296-991. PMID 8946850.
  7. ^ Schubert WD, Gobel G, Diepholz M, Darji A, Kloer D, Hain T, Chakraborty T, Wehland J, Domann E, Heinz DW (September 2001). "Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain". J. Mol. Biol. 312 (4): 783–94. doi:10.1006/jmbi.2001.4989. PMID 11575932.
  8. ^ Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E, Wehland J, Chakraborty T, Heinz DW (December 2002). "Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin". Cell. 111 (6): 825–36. doi:10.1016/S0092-8674(02)01136-4. PMID 12526809.
  9. ^ Freiberg A, Machner MP, Pfeil W, Schubert WD, Heinz DW, Seckler R (March 2004). "Folding and stability of the leucine-rich repeat domain of internalin B from Listeri monocytogenes". J. Mol. Biol. 337 (2): 453–61. doi:10.1016/j.jmb.2004.01.044. PMID 15003459.

Further reading

External links

This article incorporates text from the public domain Pfam and InterPro: IPR012569
This article incorporates text from the public domain Pfam and InterPro: IPR013210
This article incorporates text from the public domain Pfam and InterPro: IPR000372
This article incorporates text from the public domain Pfam and InterPro: IPR000483
This article incorporates text from the public domain Pfam and InterPro: IPR004830
This article incorporates text from the public domain Pfam and InterPro: IPR004830

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.

Leucine rich repeat N-terminal domain Provide feedback

Leucine Rich Repeats PF00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.

Literature references

  1. Kobe B, Deisenhofer J; , Trends Biochem Sci 1994;19:415-421.: The leucine-rich repeat: a versatile binding motif. PUBMED:7817399 EPMC:7817399


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013210

Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape [ PUBMED:14747988 ]. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [ PUBMED:11751054 , PUBMED:1657640 ].Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response [ PUBMED:2176636 , PUBMED:21606681 ].

Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is, however, now clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins, characterised by different lengths and consensus sequences of the repeats, have been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL), corresponding to the beta-strand and adjacent loop regions, are conserved in LRR proteins, whereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences, each of the variable parts contains two half-turns at both ends and a "linear" segment (as the chain follows a linear path overall), usually formed by a helix, in the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with alpha-helix, thus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions [ PUBMED:11751054 ]. Molecular modeling suggests that the conserved pattern LxxLxL, which is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats [ PUBMED:11967365 ].

This domain is often found at the N terminus of tandem leucine rich repeats, mainly in plant proteins.

Domain organisation

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

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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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  Seed
(101)
Full
(49641)
Representative proteomes UniProt
(74042)
RP15
(4145)
RP35
(26401)
RP55
(40911)
RP75
(55303)
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  Seed
(101)
Full
(49641)
Representative proteomes UniProt
(74042)
RP15
(4145)
RP35
(26401)
RP55
(40911)
RP75
(55303)
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  Seed
(101)
Full
(49641)
Representative proteomes UniProt
(74042)
RP15
(4145)
RP35
(26401)
RP55
(40911)
RP75
(55303)
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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.

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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: Pfam-B_35 (release 17.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A
Number in seed: 101
Number in full: 49641
Average length of the domain: 41.30 aa
Average identity of full alignment: 31 %
Average coverage of the sequence by the domain: 5.48 %

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 20.7 3.1
Trusted cut-off 20.7 8.1
Noise cut-off 20.6 -1000000.0
Model length: 41
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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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 LRRNT_2 domain has been found. There are 89 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
A0A0N7KCD6 View 3D Structure Click here
A0A0N7KCD8 View 3D Structure Click here
A0A0N7KEX1 View 3D Structure Click here
A0A0N7KFP1 View 3D Structure Click here
A0A0N7KIH8 View 3D Structure Click here
A0A0N7KMA0 View 3D Structure Click here
A0A0N7KMC1 View 3D Structure Click here
A0A0N7KNE6 View 3D Structure Click here
A0A0N7KRT8 View 3D Structure Click here
A0A0N7KSI2 View 3D Structure Click here
A0A0N7KSN8 View 3D Structure Click here
A0A0N7KSZ4 View 3D Structure Click here
A0A0P0UYC8 View 3D Structure Click here
A0A0P0UYE3 View 3D Structure Click here
A0A0P0UYJ1 View 3D Structure Click here
A0A0P0UYT6 View 3D Structure Click here
A0A0P0UZ20 View 3D Structure Click here
A0A0P0V387 View 3D Structure Click here
A0A0P0V4D1 View 3D Structure Click here
A0A0P0V4Y9 View 3D Structure Click here
A0A0P0V6V4 View 3D Structure Click here
A0A0P0V9M1 View 3D Structure Click here
A0A0P0VDQ9 View 3D Structure Click here
A0A0P0VET3 View 3D Structure Click here
A0A0P0VEV5 View 3D Structure Click here
A0A0P0VEW1 View 3D Structure Click here
A0A0P0VEX0 View 3D Structure Click here
A0A0P0VEY2 View 3D Structure Click here
A0A0P0VEY9 View 3D Structure Click here
A0A0P0VF17 View 3D Structure Click here
A0A0P0VF24 View 3D Structure Click here
A0A0P0VF33 View 3D Structure Click here
A0A0P0VGF8 View 3D Structure Click here
A0A0P0VHL9 View 3D Structure Click here
A0A0P0VJH3 View 3D Structure Click here
A0A0P0VSY6 View 3D Structure Click here
A0A0P0VYC3 View 3D Structure Click here
A0A0P0VZ45 View 3D Structure Click here
A0A0P0WCR3 View 3D Structure Click here
A0A0P0WFJ3 View 3D Structure Click here
A0A0P0WGW5 View 3D Structure Click here
A0A0P0WI35 View 3D Structure Click here
A0A0P0WIF5 View 3D Structure Click here
A0A0P0WIM0 View 3D Structure Click here
A0A0P0WKH3 View 3D Structure Click here
A0A0P0WNS8 View 3D Structure Click here
A0A0P0WTA7 View 3D Structure Click here
A0A0P0WTB4 View 3D Structure Click here
A0A0P0WTL7 View 3D Structure Click here
A0A0P0WV71 View 3D Structure Click here
A0A0P0WY19 View 3D Structure Click here
A0A0P0WYI2 View 3D Structure Click here
A0A0P0WYL7 View 3D Structure Click here
A0A0P0WYQ5 View 3D Structure Click here
A0A0P0X077 View 3D Structure Click here
A0A0P0X811 View 3D Structure Click here
A0A0P0XDF8 View 3D Structure Click here
A0A0P0XDT2 View 3D Structure Click here
A0A0P0XG73 View 3D Structure Click here
A0A0P0XMC8 View 3D Structure Click here
A0A0P0XR54 View 3D Structure Click here
A0A0P0XTU7 View 3D Structure Click here
A0A0P0XU58 View 3D Structure Click here
A0A0P0XUL8 View 3D Structure Click here
A0A0P0XV52 View 3D Structure Click here
A0A0P0XV54 View 3D Structure Click here
A0A0P0XZM1 View 3D Structure Click here
A0A0P0Y095 View 3D Structure Click here
A0A0P0Y0Y5 View 3D Structure Click here
A0A0P0Y1X0 View 3D Structure Click here
A0A0P0Y2E2 View 3D Structure Click here
A0A0P0Y2U8 View 3D Structure Click here
A0A0P0Y3E8 View 3D Structure Click here
A0A0P0Y3G4 View 3D Structure Click here
A0A0P0Y3G5 View 3D Structure Click here
A0A0P0Y3J7 View 3D Structure Click here
A0A0P0Y3K7 View 3D Structure Click here
A0A0P0Y3Q8 View 3D Structure Click here
A0A0P0Y4V7 View 3D Structure Click here
A0A0P0Y5A4 View 3D Structure Click here
A0A0P0Y5T8 View 3D Structure Click here
A0A0P0Y5V7 View 3D Structure Click here
A0A0P0Y814 View 3D Structure Click here
A0A0P0Y873 View 3D Structure Click here
A0A0P0Y8A4 View 3D Structure Click here
A0A0P0Y8B7 View 3D Structure Click here
A0A0P0Y8C7 View 3D Structure Click here
A0A0P0Y8G5 View 3D Structure Click here
A0A0P0Y8G9 View 3D Structure Click here
A0A0P0Y8Y6 View 3D Structure Click here
A0A0P0YE31 View 3D Structure Click here
A0A0R0E2L7 View 3D Structure Click here
A0A0R0E2R8 View 3D Structure Click here
A0A0R0E3W6 View 3D Structure Click here
A0A0R0E484 View 3D Structure Click here
A0A0R0E9I8 View 3D Structure Click here
A0A0R0EE32 View 3D Structure Click here
A0A0R0EEJ3 View 3D Structure Click here
A0A0R0EH14 View 3D Structure Click here
A0A0R0EML4 View 3D Structure Click here
A0A0R0ETU4 View 3D Structure Click here
A0A0R0EYN3 View 3D Structure Click here
A0A0R0F1S7 View 3D Structure Click here
A0A0R0F1Z8 View 3D Structure Click here
A0A0R0F288 View 3D Structure Click here
A0A0R0F4Z2 View 3D Structure Click here
A0A0R0F4Z2 View 3D Structure Click here
A0A0R0F9Q1 View 3D Structure Click here
A0A0R0FAU2 View 3D Structure Click here
A0A0R0FBM0 View 3D Structure Click here
A0A0R0FD00 View 3D Structure Click here
A0A0R0FDC0 View 3D Structure Click here
A0A0R0FEJ4 View 3D Structure Click here
A0A0R0FEP8 View 3D Structure Click here
A0A0R0FGS7 View 3D Structure Click here
A0A0R0FM78 View 3D Structure Click here
A0A0R0FM79 View 3D Structure Click here
A0A0R0FMR6 View 3D Structure Click here
A0A0R0FP46 View 3D Structure Click here
A0A0R0FPY0 View 3D Structure Click here
A0A0R0FPY4 View 3D Structure Click here
A0A0R0FPZ4 View 3D Structure Click here
A0A0R0FQ38 View 3D Structure Click here
A0A0R0FQ61 View 3D Structure Click here
A0A0R0FRM6 View 3D Structure Click here
A0A0R0FRN7 View 3D Structure Click here
A0A0R0FRQ4 View 3D Structure Click here
A0A0R0FRS0 View 3D Structure Click here
A0A0R0FRU8 View 3D Structure Click here
A0A0R0FRV6 View 3D Structure Click here
A0A0R0FS17 View 3D Structure Click here
A0A0R0FS75 View 3D Structure Click here
A0A0R0FS76 View 3D Structure Click here
A0A0R0FS91 View 3D Structure Click here
A0A0R0FS93 View 3D Structure Click here
A0A0R0FS98 View 3D Structure Click here
A0A0R0FSA0 View 3D Structure Click here
A0A0R0FSB0 View 3D Structure Click here
A0A0R0FSB3 View 3D Structure Click here
A0A0R0FSB5 View 3D Structure Click here
A0A0R0FSC7 View 3D Structure Click here
A0A0R0FSE4 View 3D Structure Click here
A0A0R0FSE6 View 3D Structure Click here
A0A0R0FSE9 View 3D Structure Click here
A0A0R0FSF4 View 3D Structure Click here
A0A0R0FSF9 View 3D Structure Click here
A0A0R0FSI0 View 3D Structure Click here
A0A0R0FSJ5 View 3D Structure Click here
A0A0R0FSN3 View 3D Structure Click here
A0A0R0FSQ9 View 3D Structure Click here
A0A0R0FSW0 View 3D Structure Click here
A0A0R0FSX4 View 3D Structure Click here
A0A0R0FVL3 View 3D Structure Click here
A0A0R0FWJ6 View 3D Structure Click here
A0A0R0FYG0 View 3D Structure Click here
A0A0R0FYQ0 View 3D Structure Click here
A0A0R0FYR4 View 3D Structure Click here
A0A0R0FYS8 View 3D Structure Click here
A0A0R0FZ28 View 3D Structure Click here
A0A0R0FZK4 View 3D Structure Click here
A0A0R0FZM3 View 3D Structure Click here
A0A0R0FZV5 View 3D Structure Click here
A0A0R0G097 View 3D Structure Click here
A0A0R0G0A6 View 3D Structure Click here
A0A0R0G0D9 View 3D Structure Click here
A0A0R0G0H2 View 3D Structure Click here
A0A0R0G0L3 View 3D Structure Click here
A0A0R0G0N8 View 3D Structure Click here
A0A0R0G127 View 3D Structure Click here
A0A0R0G143 View 3D Structure Click here
A0A0R0G173 View 3D Structure Click here
A0A0R0G196 View 3D Structure Click here
A0A0R0G198 View 3D Structure Click here
A0A0R0G1D2 View 3D Structure Click here
A0A0R0G1F4 View 3D Structure Click here
A0A0R0G1S2 View 3D Structure Click here
A0A0R0G1Y5 View 3D Structure Click here
A0A0R0G217 View 3D Structure Click here
A0A0R0G2C1 View 3D Structure Click here
A0A0R0G2K3 View 3D Structure Click here
A0A0R0G349 View 3D Structure Click here
A0A0R0G365 View 3D Structure Click here
A0A0R0G3A6 View 3D Structure Click here
A0A0R0G3Q3 View 3D Structure Click here
A0A0R0G3T0 View 3D Structure Click here
A0A0R0G3X8 View 3D Structure Click here
A0A0R0G4R8 View 3D Structure Click here
A0A0R0G607 View 3D Structure Click here
A0A0R0G608 View 3D Structure Click here
A0A0R0G850 View 3D Structure Click here
A0A0R0G940 View 3D Structure Click here
A0A0R0G9R2 View 3D Structure Click here
A0A0R0GEL6 View 3D Structure Click here
A0A0R0GEU9 View 3D Structure Click here
A0A0R0GFK8 View 3D Structure Click here
A0A0R0GHH6 View 3D Structure Click here
A0A0R0GI87 View 3D Structure Click here
A0A0R0GIF6 View 3D Structure Click here
A0A0R0GIG3 View 3D Structure Click here
A0A0R0GIQ7 View 3D Structure Click here
A0A0R0GIX6 View 3D Structure Click here
A0A0R0GIZ1 View 3D Structure Click here
A0A0R0GJ65 View 3D Structure Click here
A0A0R0GKL0 View 3D Structure Click here
A0A0R0GL67 View 3D Structure Click here
A0A0R0GLN1 View 3D Structure Click here
A0A0R0H291 View 3D Structure Click here
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