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1EAI

COMPLEX OF ASCARIS CHYMOTRPSIN/ELASTASE INHIBITOR WITH PORCINE ELASTASE

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
C0004867molecular_functionserine-type endopeptidase inhibitor activity
C0005576cellular_componentextracellular region
D0004867molecular_functionserine-type endopeptidase inhibitor activity
D0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idREC
Number of Residues2
DetailsREACTIVE SITE
ChainResidue
CLEU31
CMET32

site_idRED
Number of Residues2
DetailsREACTIVE SITE
ChainResidue
DLEU31
DMET32

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. MTAAHC
ChainResidueDetails
AMET53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SGcqGDSGGPLH
ChainResidueDetails
ASER189-HIS200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Reactive bond => ECO:0000305|PubMed:7922044
ChainResidueDetails
CLEU31
DLEU31

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:5415110
ChainResidueDetails
AASP102
ASER195
BASP102
BSER195

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
AGLU70
AASN72
AGLN75
AGLU80
BGLU70
BASN72
BGLN75
BGLU80

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57
AGLY196

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

site_idCSA7
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57
ASER214

site_idCSA8
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57
BSER214

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PDB entries from 2024-07-24

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