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1ELD

Structural analysis of the active site of porcine pancreatic elastase based on the x-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors

Functional Information from GO Data
ChainGOidnamespacecontents
E0004252molecular_functionserine-type endopeptidase activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0006508biological_processproteolysis
E0008236molecular_functionserine-type peptidase activity
E0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 0Z0 E 256
ChainResidue
EHIS60
ETHR221
ESER222
EPHE223
EVAL224
EARG226
EACY300
EHOH642
EHOH651
EGLU65
ELEU66
EVAL103
EALA104
ETHR182
ECYS199
EGLN200
ESER203

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 280
ChainResidue
EGLU74
EASN76
EGLN79
EASN81
EGLU84
EHOH327

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY E 300
ChainResidue
ETHR44
EHIS60
EGLN200
EGLY201
ESER203
E0Z0256
EHOH647

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. MTAAHC
ChainResidueDetails
EMET56-CYS61

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SGcqGDSGGPLH
ChainResidueDetails
ESER197-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
EHIS60

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:5415110
ChainResidueDetails
EASP108
ESER203

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
EGLU74
EASN76
EGLN79
EGLU84

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EHIS60
EASP108

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EGLY204
ESER203

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EGLY201
ESER203

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EHIS60
ESER203
EASP108

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EGLY204
EHIS60
ESER203
EASP108

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EGLY201
EHIS60
ESER203
EASP108

site_idCSA7
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EGLY201
EHIS60
ESER222
ESER203
EASP108

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PDB entries from 2024-07-10

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