Structure of PDB 2erq Chain B

Receptor sequence
>2erqB (length=423) Species: 8730 (Crotalus atrox) [Search protein sequence]
LTPEQQRYLNAKKYVKLFLVADYIMYLKYGRNLTAVRTRMYDIVNVITPI
YHRMNIHVALVGLEIWSNTDKIIVQSSADVTLDLFAKWRATDLLSRKSHD
NAQLLTGINFNGPTAGLGYLGGICNTMYSAGIVQDHSKIHHLVAIAMAHE
MGHNLGMDHDKDTCTCGTRPCVMAGALSCEASFLFSDCSQKDHREFLIKN
MPQCILKKPLKTDVVSPAVCGNYFVEVGEECDCGSPRTCRDPCCDATTCK
LRQGAQCAEGLCCDQCRFKGAGTECRAAKDECDMADVCTGRSAECTDRFQ
RNGQPCKNNNGYCYNGKCPIMADQCIALFGPGATVSQDACFQFNREGNHY
GYCRKEQNTKIACEPQDVKCGRLYCFPNSPENKNPCNIYYSPNDEDKGMV
LPGTKCADRKACSNGQCVDVTTP
3D structure
PDB2erq Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold
ChainB
Resolution2.5 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 ZN B H335 H339 H345 H149 H153 H159
BS02 CA B V405 N408 F410 E412 E415 D418 V219 N222 F224 E226 E229 D232
BS03 CA B D469 M470 D472 D483 R484 D283 M284 D286 D297 R298
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:2erq, PDBe:2erq, PDBj:2erq
PDBsum2erq
PubMed16688218
UniProtQ9DGB9|VM3V1_CROAT Zinc metalloproteinase-disintegrin-like VAP1

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