Structure of PDB 3sbk Chain A

Receptor sequence
>3sbkA (length=234) Species: 343250 (Daboia siamensis) [Search protein sequence]
VVGGDECNINEHPFLVALYTSASSTIHCAGALINREWVLTAAHCDRRNIR
IKLGMHSKNIRNEDEQIRVPRGKYFCLNTKFPNGLDKDIMLIRLRRPVTY
STHIAPVSLPSRSRGVGSRCRIMGWGKISTTTYPDVPHCTNIFIVKHKWC
EPLYPWVPADSRTLCAGILKGGRDTCHGDSGGPLICNGEMHGIVAGGSEP
CGQHLKPAVYTKVFDYNNWIQSIIAGNRTVTCPP
3D structure
PDB3sbk Structural basis of coagulation factor V recognition for cleavage by RVV-V
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 H192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H43 D88 H177 G178 D179 S180 G181
Enzyme Commision number 3.4.21.95: snake venom factor V activator.
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 0G6 A H57 Y172 D189 T190 C191 S195 A214 G215 G216 S217 E218 H43 Y154 D174 T175 C176 S180 A195 G196 G197 S198 E199
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0090729 toxin activity
Biological Process
GO:0006508 proteolysis
GO:0035821 modulation of process of another organism
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3sbk, PDBe:3sbk, PDBj:3sbk
PDBsum3sbk
PubMed21871889
UniProtP18965|VSPG_DABSI Factor V activator RVV-V gamma

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