Structure of PDB 2cv3 Chain A

Receptor sequence
>2cv3A (length=240) Species: 9823 (Sus scrofa) [Search protein sequence]
VVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRE
LTFRVVVGEHNLNQNDGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLA
QSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYL
PTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQY
AVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN
3D structure
PDB2cv3 Structure of the complex of porcine pancreatic elastase with a trimacrocyclic peptide inhibitor FR901451
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H60 D108 Q200 G201 D202 S203 G204
Catalytic site (residue number reindexed from 1) H45 D93 Q185 G186 D187 S188 G189
Enzyme Commision number 3.4.21.36: pancreatic elastase.
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 peptide A Y35 T44 C45 H60 R64 L66 L149 L156 G198 C199 Q200 G201 S203 S222 F223 V224 R226 Y20 T29 C30 H45 R49 L51 L134 L141 G183 C184 Q185 G186 S188 S207 F208 V209 R211
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
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:2cv3, PDBe:2cv3, PDBj:2cv3
PDBsum2cv3
PubMed16511165
UniProtP00772|CELA1_PIG Chymotrypsin-like elastase family member 1 (Gene Name=CELA1)

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