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1OKX

Binding Structure of Elastase Inhibitor Scyptolin A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0046872molecular_functionmetal ion binding
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR CHAIN C OF SCYPTOLIN A
ChainResidue
ATHR44
ASER203
ATHR221
ASER222
APHE223
AVAL224
ASER225
AARG226
AHOH2014
BLEU149
BASN153
ACYS45
BGLY154
BGLN200
CHOH2001
CHOH2002
DCNT1262
AHIS60
AVAL103
AGLY198
ACYS199
AGLN200
AGLY201
AASP202

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR CHAIN D OF SCYPTOLIN A
ChainResidue
AASN153
AGLN200
AARG226
BTHR44
BCYS45
BHIS60
BVAL103
BGLY198
BCYS199
BGLN200
BGLY201
BASP202
BSER203
BTHR221
BSER222
BPHE223
BVAL224
BSER225
BARG226
CTHR1258
CCNT1262
DHOH2001
DHOH2002

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 Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:4578945, ECO:0000269|PubMed:5415110
ChainResidueDetails
AHIS60
BHIS60

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:5415110
ChainResidueDetails
AASP108
ASER203
BASP108
BSER203

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:7656008, ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, ECO:0007744|PDB:1ELC
ChainResidueDetails
AGLU74
AASN76
AGLN79
AGLU84
BGLU74
BASN76
BGLN79
BGLU84

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AHIS60
ASER203
AASP108

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BHIS60
BSER203
BASP108

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY201
AHIS60
ASER203
AASP108

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BGLY201
BHIS60
BSER203
BASP108

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY204
AHIS60
ASER203
AASP108

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BGLY204
BHIS60
BSER203
BASP108

site_idCSA7
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY201
AHIS60
ASER222
ASER203
AASP108

site_idCSA8
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BGLY201
BHIS60
BSER222
BSER203
BASP108

223532

PDB entries from 2024-08-07

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