1K32
Crystal structure of the tricorn protease
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006508 | biological_process | proteolysis |
B | 0008233 | molecular_function | peptidase activity |
B | 0008236 | molecular_function | serine-type peptidase activity |
B | 0016787 | molecular_function | hydrolase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006508 | biological_process | proteolysis |
C | 0008233 | molecular_function | peptidase activity |
C | 0008236 | molecular_function | serine-type peptidase activity |
C | 0016787 | molecular_function | hydrolase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006508 | biological_process | proteolysis |
D | 0008233 | molecular_function | peptidase activity |
D | 0008236 | molecular_function | serine-type peptidase activity |
D | 0016787 | molecular_function | hydrolase activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0006508 | biological_process | proteolysis |
E | 0008233 | molecular_function | peptidase activity |
E | 0008236 | molecular_function | serine-type peptidase activity |
E | 0016787 | molecular_function | hydrolase activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0006508 | biological_process | proteolysis |
F | 0008233 | molecular_function | peptidase activity |
F | 0008236 | molecular_function | serine-type peptidase activity |
F | 0016787 | molecular_function | hydrolase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1626 |
Details | Region: {"description":"Six-bladed beta propeller","evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | Region: {"description":"Binds the substrate's C-terminus","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2094 |
Details | Region: {"description":"Seven-bladed beta propeller","evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 396 |
Details | Region: {"description":"C-1; helical bundle","evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 564 |
Details | Region: {"description":"PDZ-like","evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1230 |
Details | Region: {"description":"C-2; alpha-beta sandwich","evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 6 |
Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 6 |
Details | Site: {"description":"Substrate specificity switch","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 6 |
Details | Site: {"description":"Transition state stabilizer; via amide nitrogen","evidences":[{"source":"PubMed","id":"11719810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12470958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 11719810 |
Chain | Residue | Details |
A | SER965 | |
A | HIS746 | |
A | ASP966 | |
A | GLY918 |
site_id | CSA2 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 11719810 |
Chain | Residue | Details |
B | SER965 | |
B | HIS746 | |
B | ASP966 | |
B | GLY918 |
site_id | CSA3 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 11719810 |
Chain | Residue | Details |
C | SER965 | |
C | HIS746 | |
C | ASP966 | |
C | GLY918 |
site_id | CSA4 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 11719810 |
Chain | Residue | Details |
D | SER965 | |
D | HIS746 | |
D | ASP966 | |
D | GLY918 |
site_id | CSA5 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 11719810 |
Chain | Residue | Details |
E | SER965 | |
E | HIS746 | |
E | ASP966 | |
E | GLY918 |
site_id | CSA6 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 11719810 |
Chain | Residue | Details |
F | SER965 | |
F | HIS746 | |
F | ASP966 | |
F | GLY918 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 808 |
Chain | Residue | Details |
A | HIS746 | proton shuttle (general acid/base) |
A | GLY918 | electrostatic stabiliser |
A | SER965 | covalently attached |
A | ASP966 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 808 |
Chain | Residue | Details |
B | HIS746 | proton shuttle (general acid/base) |
B | GLY918 | electrostatic stabiliser |
B | SER965 | covalently attached |
B | ASP966 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 808 |
Chain | Residue | Details |
C | HIS746 | proton shuttle (general acid/base) |
C | GLY918 | electrostatic stabiliser |
C | SER965 | covalently attached |
C | ASP966 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 808 |
Chain | Residue | Details |
D | HIS746 | proton shuttle (general acid/base) |
D | GLY918 | electrostatic stabiliser |
D | SER965 | covalently attached |
D | ASP966 | electrostatic stabiliser |
site_id | MCSA5 |
Number of Residues | 4 |
Details | M-CSA 808 |
Chain | Residue | Details |
E | HIS746 | proton shuttle (general acid/base) |
E | GLY918 | electrostatic stabiliser |
E | SER965 | covalently attached |
E | ASP966 | electrostatic stabiliser |
site_id | MCSA6 |
Number of Residues | 4 |
Details | M-CSA 808 |
Chain | Residue | Details |
F | HIS746 | proton shuttle (general acid/base) |
F | GLY918 | electrostatic stabiliser |
F | SER965 | covalently attached |
F | ASP966 | electrostatic stabiliser |