Structure of PDB 2cv3 Chain A Binding Site BS01
Receptor Information
>2cv3 Chain A (length=240) Species:
9823
(Sus scrofa) [
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VVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRE
LTFRVVVGEHNLNQNDGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLA
QSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYL
PTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQY
AVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN
Ligand information
>2cv3 Chain B (length=11) Species:
1005
(Flexibacter sp.) [
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TTLKFPSDWDD
Receptor-Ligand Complex Structure
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PDB
2cv3
Structure of the complex of porcine pancreatic elastase with a trimacrocyclic peptide inhibitor FR901451
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
Y35 T44 C45 H60 R64 L66 L149 L156 G198 C199 Q200 G201 S203 S222 F223 V224 R226
Binding residue
(residue number reindexed from 1)
Y20 T29 C30 H45 R49 L51 L134 L141 G183 C184 Q185 G186 S188 S207 F208 V209 R211
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.
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
PDBsum
2cv3
PubMed
16511165
UniProt
P00772
|CELA1_PIG Chymotrypsin-like elastase family member 1 (Gene Name=CELA1)
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