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2GDD

Human beta II tryptase with inhibitor CRA-27592

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0031012cellular_componentextracellular matrix
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016787molecular_functionhydrolase activity
B0031012cellular_componentextracellular matrix
C0004252molecular_functionserine-type endopeptidase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008236molecular_functionserine-type peptidase activity
C0016787molecular_functionhydrolase activity
C0031012cellular_componentextracellular matrix
D0004252molecular_functionserine-type endopeptidase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008236molecular_functionserine-type peptidase activity
D0016787molecular_functionhydrolase activity
D0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 5AM A 999
ChainResidue
AVAL35
AGLN192
AGLY193
AASP194
ASER195
ASER214
ATRP215
AHOH1035
APHE41
AHIS57
ACYS58
ALYS60
ALEU64
AASP189
ASER190
ACYS191

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 5AM B 998
ChainResidue
BPHE41
BHIS57
BCYS58
BLYS60
BLEU64
BASP189
BSER190
BCYS191
BGLN192
BGLY193
BASP194
BSER195
BVAL213
BSER214
BTRP215
BGLY226
BHOH1008
BHOH1016

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 5AM C 997
ChainResidue
CPHE41
CHIS57
CCYS58
CVAL59
CLYS60
CLEU64
CASP189
CSER190
CCYS191
CGLN192
CGLY193
CASP194
CSER195
CSER214
CTRP215
CGLY219
CGLY226
CHOH1021

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 5AM D 996
ChainResidue
DPHE41
DHIS57
DCYS58
DLYS60
DASP60
DLEU64
DASP189
DSER190
DCYS191
DGLN192
DGLY193
DASP194
DSER195
DSER214
DTRP215
DHOH1003
DHOH1010

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU53-CYS58

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues964
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":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P21845","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

site_idCSA10
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

site_idCSA11
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CHIS57
CGLY196

site_idCSA12
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DHIS57
DGLY196

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

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CHIS57

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CGLY193
CHIS57

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DGLY193
DHIS57

site_idCSA9
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57
AGLY196

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PDB entries from 2025-08-27

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