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1K32

Crystal structure of the tricorn protease

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016787molecular_functionhydrolase activity
C0005737cellular_componentcytoplasm
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008236molecular_functionserine-type peptidase activity
C0016787molecular_functionhydrolase activity
D0005737cellular_componentcytoplasm
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008236molecular_functionserine-type peptidase activity
D0016787molecular_functionhydrolase activity
E0005737cellular_componentcytoplasm
E0006508biological_processproteolysis
E0008233molecular_functionpeptidase activity
E0008236molecular_functionserine-type peptidase activity
E0016787molecular_functionhydrolase activity
F0005737cellular_componentcytoplasm
F0006508biological_processproteolysis
F0008233molecular_functionpeptidase activity
F0008236molecular_functionserine-type peptidase activity
F0016787molecular_functionhydrolase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1626
DetailsRegion: {"description":"Six-bladed beta propeller","evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsRegion: {"description":"Binds the substrate's C-terminus","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2094
DetailsRegion: {"description":"Seven-bladed beta propeller","evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues396
DetailsRegion: {"description":"C-1; helical bundle","evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues564
DetailsRegion: {"description":"PDZ-like","evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1230
DetailsRegion: {"description":"C-2; alpha-beta sandwich","evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues6
DetailsSite: {"description":"Substrate specificity switch","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues6
DetailsSite: {"description":"Transition state stabilizer; via amide nitrogen","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 11719810
ChainResidueDetails
ASER965
AHIS746
AASP966
AGLY918

site_idCSA2
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 11719810
ChainResidueDetails
BSER965
BHIS746
BASP966
BGLY918

site_idCSA3
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 11719810
ChainResidueDetails
CSER965
CHIS746
CASP966
CGLY918

site_idCSA4
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 11719810
ChainResidueDetails
DSER965
DHIS746
DASP966
DGLY918

site_idCSA5
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 11719810
ChainResidueDetails
ESER965
EHIS746
EASP966
EGLY918

site_idCSA6
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 11719810
ChainResidueDetails
FSER965
FHIS746
FASP966
FGLY918

site_idMCSA1
Number of Residues4
DetailsM-CSA 808
ChainResidueDetails
AHIS746proton shuttle (general acid/base)
AGLY918electrostatic stabiliser
ASER965covalently attached
AASP966electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 808
ChainResidueDetails
BHIS746proton shuttle (general acid/base)
BGLY918electrostatic stabiliser
BSER965covalently attached
BASP966electrostatic stabiliser

site_idMCSA3
Number of Residues4
DetailsM-CSA 808
ChainResidueDetails
CHIS746proton shuttle (general acid/base)
CGLY918electrostatic stabiliser
CSER965covalently attached
CASP966electrostatic stabiliser

site_idMCSA4
Number of Residues4
DetailsM-CSA 808
ChainResidueDetails
DHIS746proton shuttle (general acid/base)
DGLY918electrostatic stabiliser
DSER965covalently attached
DASP966electrostatic stabiliser

site_idMCSA5
Number of Residues4
DetailsM-CSA 808
ChainResidueDetails
EHIS746proton shuttle (general acid/base)
EGLY918electrostatic stabiliser
ESER965covalently attached
EASP966electrostatic stabiliser

site_idMCSA6
Number of Residues4
DetailsM-CSA 808
ChainResidueDetails
FHIS746proton shuttle (general acid/base)
FGLY918electrostatic stabiliser
FSER965covalently attached
FASP966electrostatic stabiliser

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PDB entries from 2025-07-30

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