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1A0J

CRYSTAL STRUCTURE OF A NON-PSYCHROPHILIC TRYPSIN FROM A COLD-ADAPTED FISH SPECIES.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0007586biological_processdigestion
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0004252molecular_functionserine-type endopeptidase activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0007586biological_processdigestion
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0004252molecular_functionserine-type endopeptidase activity
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006508biological_processproteolysis
C0007586biological_processdigestion
C0008233molecular_functionpeptidase activity
C0008236molecular_functionserine-type peptidase activity
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0004252molecular_functionserine-type endopeptidase activity
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0006508biological_processproteolysis
D0007586biological_processdigestion
D0008233molecular_functionpeptidase activity
D0008236molecular_functionserine-type peptidase activity
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 247
ChainResidue
AGLU70
AASN72
AVAL75
AGLU77
AGLU80

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 248
ChainResidue
ASER195
AHIS40
AHIS57
AGLN192
AGLY193

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 249
ChainResidue
APRO152
AASP153
ATHR154
AARG156

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 248
ChainResidue
BHIS57
BGLN192
BGLY193
BSER195
BBEN246
BHOH323

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 249
ChainResidue
BPRO152
BASP153
BTHR154
BARG156

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 248
ChainResidue
CHIS57
CGLN192
CGLY193
CSER195
CBEN246
CHOH614

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 249
ChainResidue
CGLU21
CPRO152
CASP153
CTHR154
CARG156

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 248
ChainResidue
ATYR39
DHIS57
DGLN192
DGLY193
DSER195
DBEN246

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 249
ChainResidue
AASN76
BARG235
DPRO152
DASP153
DTHR154
DARG156

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 250
ChainResidue
ASER148
ASER149
CASN95
CARG97
DARG62
DHOH490

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 251
ChainResidue
CSER96
DLYS60
DSER61
DHOH474
DHOH503

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BEN A 246
ChainResidue
AASP189
ASER190
ASER195
AGLY219
ACYS220
AGLY226

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BEN B 246
ChainResidue
BASP189
BSER190
BSER195
BGLY219
BGLY226
BSO4248

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BEN C 246
ChainResidue
CASP189
CSER190
CCYS191
CSER195
CGLY219
CGLY226
CSO4248
CHOH312

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BEN D 246
ChainResidue
DASP189
DSER190
DCYS191
DSER195
DGLY219
DGLY226
DSO4248

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV
ChainResidueDetails
AASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues880
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsActive site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Required for specificity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 11948789
ChainResidueDetails
ASER195
ASER195
AHIS57
AASP102
AGLY193

240971

PDB entries from 2025-08-27

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