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2CV3

Crystal structure of porcine pancreatic elastase complexed with a macroclyclic peptide inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues30
DetailsBINDING SITE FOR CHAIN B OF INHIBITOR FR901451
ChainResidue
ATYR35
AGLY198
ACYS199
AGLN200
AGLY201
AASP202
ASER203
ASER222
APHE223
AVAL224
ASER225
ATHR44
AARG226
AHOH340
AHOH405
AHOH473
BHOH279
BHOH314
BHOH318
BHOH331
BHOH380
BHOH416
ACYS45
BHOH538
AHIS60
ACYS61
AARG64
ALEU66
ALYS91
ALEU149

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. MTAAHC
ChainResidueDetails
AMET56-CYS61

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SGcqGDSGGPLH
ChainResidueDetails
ASER197-HIS208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:4578945, ECO:0000269|PubMed:5415110
ChainResidueDetails
AHIS60

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:5415110
ChainResidueDetails
AASP108
ASER203

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:7656008, ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, ECO:0007744|PDB:1ELC
ChainResidueDetails
AGLU74
AASN76
AGLN79
AGLU84

218853

PDB entries from 2024-04-24

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