Structure of PDB 2vqx Chain A

Receptor sequence
>2vqxA (length=322) Species: 28151 (Serratia proteamaculans) [Search protein sequence]
ARSVIPPYMLRRIIEHGSLPQRDCALHTLNHVKTSTGGEVIRDIYDAENS
TQLPGKQVRNEGQASNHDVAVDEAYDYLGVTYDFFWQAFKRNSLDNQGLP
LTGSVHYGKEYQNAFWNGQQMVFGDGDGEIFNRFTIAIDVVGHALAHGVT
ESEAGLIYFQQAGALNESLSDVFGSLVKQFHLKQTADKADWLIGEGLLAK
GINGKGLRSMSAPGTAYDDPLLGKDPQPASMKDYIQTKEDNGGVHLNSGI
PNRAFYLAATALGGYAWEKAGYIWYDTLCDKALPQDADFATFARTTVKHA
EQRFDSKVAQKVQQAWHQVGVA
3D structure
PDB2vqx Crystal Structure of the Protealysin Precursor: Insights Into Propeptide Function.
ChainA
Resolution1.821 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H162 A163 H166 Y177 E186 D259 H264
Catalytic site (residue number reindexed from 1) H143 A144 H147 Y158 E167 D240 H245
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 A H162 H166 E186 H143 H147 E167
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:2vqx, PDBe:2vqx, PDBj:2vqx
PDBsum2vqx
PubMed19915005
UniProtQ5MJ80

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