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1TRN

CRYSTAL STRUCTURE OF HUMAN TRYPSIN 1: UNEXPECTED PHOSPHORYLATION OF TYROSINE 151

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0007586biological_processdigestion
A0008236molecular_functionserine-type peptidase activity
A0022617biological_processextracellular matrix disassembly
A0046872molecular_functionmetal ion binding
A0062023cellular_componentcollagen-containing extracellular matrix
A0072562cellular_componentblood microparticle
B0004252molecular_functionserine-type endopeptidase activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0007586biological_processdigestion
B0008236molecular_functionserine-type peptidase activity
B0022617biological_processextracellular matrix disassembly
B0046872molecular_functionmetal ion binding
B0062023cellular_componentcollagen-containing extracellular matrix
B0072562cellular_componentblood microparticle
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ISP A 301
ChainResidue
AGLY193
AASP194
ASER195
AVAL213
AHIS57
ACYS191
AGLN192

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ISP B 301
ChainResidue
BHIS57
BCYS191
BGLN192
BGLY193
BASP194
BSER195
BVAL213
BSER214

site_idCAT
Number of Residues6
Details
ChainResidue
ASER195
AHIS57
AASP102
BSER195
BHIS57
BASP102

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAGHC
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 Residues6
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
ASER195
BHIS57
BASP102
BSER195

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLU70
AASN72
AVAL75
AGLU80
BGLU70
BASN72
BVAL75
BGLU80

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Required for specificity => ECO:0000250
ChainResidueDetails
AASP189
BASP189

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Sulfotyrosine => ECO:0000305|PubMed:17087724, ECO:0000305|PubMed:25010489
ChainResidueDetails
APTR151
BPTR151

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

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PDB entries from 2024-07-10

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