Structure of PDB 2dw2 Chain B

Receptor sequence
>2dw2B (length=415) Species: 8730 (Crotalus atrox) [Search protein sequence]
NPFRFVELVLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYMYIHVA
LVGLEIWSNEDKITVKPEAGYTLNAFGEWRKTDLLTRKKHDNAQLLTAID
LDRVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHD
SGYCSCGDYACIMRPEISPEPSTFFSNCSYFECWDFIMNHNPECILNEPL
GTDIISPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHG
DCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDN
YGYCYNGNCPIMYHQCYDLFGADVYEAEDSCFERNQKGNYYGYCRKENGN
KIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNEDEHKGMVLPGTKCADG
KVCSNGHCVDVATAY
3D structure
PDB2dw2 Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins
ChainB
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.24.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MAN B S464 E465 S270 E271
BS02 ZN B H333 H337 H343 H139 H143 H149
BS03 CA B E201 D285 C388 N391 E7 D91 C194 N197
BS04 CA B V403 N406 L408 E410 E413 D416 V209 N212 L214 E216 E219 D222
BS05 CA B D467 P468 E470 D482 V483 D273 P274 E276 D288 V289
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2dw2, PDBe:2dw2, PDBj:2dw2
PDBsum2dw2
PubMed17485084
UniProtQ90282|VM3VB_CROAT Zinc metalloproteinase-disintegrin-like VAP2B

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