Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006508 | biological_process | proteolysis |
A | 0008234 | molecular_function | cysteine-type peptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 601 |
Chain | Residue |
B | CYS25 |
B | HIS164 |
B | GNQ501 |
B | CL801 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 602 |
Chain | Residue |
B | ASP139 |
B | HIS142 |
B | HOH882 |
B | HOH933 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 603 |
Chain | Residue |
B | GLU15 |
B | HIS188 |
B | GLU193 |
A | ASP173 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 701 |
Chain | Residue |
A | CYS25 |
A | HIS164 |
A | GNQ401 |
A | CL802 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 702 |
Chain | Residue |
A | ASP139 |
A | HIS142 |
A | HOH803 |
A | HOH940 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 703 |
Chain | Residue |
A | ASP3 |
A | HOH864 |
A | HOH926 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL B 801 |
Chain | Residue |
B | GLN19 |
B | CYS25 |
B | HIS164 |
B | TRP186 |
B | GNQ501 |
B | ZN601 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 802 |
Chain | Residue |
A | GLN19 |
A | CYS25 |
A | HIS164 |
A | TRP186 |
A | GNQ401 |
A | ZN701 |
site_id | AC9 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE GNQ A 401 |
Chain | Residue |
A | CYS25 |
A | TRP26 |
A | GLY62 |
A | LYS64 |
A | GLY68 |
A | GLY69 |
A | PHE70 |
A | ALA140 |
A | ARG141 |
A | HIS142 |
A | TYR154 |
A | VAL162 |
A | ASN163 |
A | HIS164 |
A | GLY165 |
A | TRP186 |
A | PHE211 |
A | ZN701 |
A | CL802 |
A | HOH892 |
B | HIS142 |
B | PRO143 |
B | PHE146 |
B | GNQ501 |
site_id | BC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE GNQ B 501 |
Chain | Residue |
A | HIS142 |
A | PRO143 |
A | PHE146 |
A | GNQ401 |
B | CYS25 |
B | TRP26 |
B | GLY62 |
B | LYS64 |
B | ASN67 |
B | GLY68 |
B | GLY69 |
B | PHE70 |
B | ALA140 |
B | ARG141 |
B | HIS142 |
B | TYR154 |
B | VAL162 |
B | ASN163 |
B | HIS164 |
B | GLY165 |
B | TRP186 |
B | PHE211 |
B | ZN601 |
B | CL801 |
Functional Information from PROSITE/UniProt
site_id | PS00139 |
Number of Residues | 12 |
Details | THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGACWAfSA |
Chain | Residue | Details |
B | GLN19-ALA30 | |
site_id | PS00639 |
Number of Residues | 11 |
Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VNHGVLVVGYG |
Chain | Residue | Details |
B | VAL162-GLY172 | |
site_id | PS00640 |
Number of Residues | 20 |
Details | THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWghnFGeeGYIrM |
Chain | Residue | Details |
B | TYR179-MET198 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
B | CYS25 | |
B | HIS164 | |
B | ASN184 | |
A | CYS25 | |
A | HIS164 | |
A | ASN184 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
B | HIS164 | |
B | CYS25 | |
B | ASN184 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
A | HIS164 | |
A | CYS25 | |
A | ASN184 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
B | HIS164 | |
B | GLN19 | |
B | CYS25 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
A | HIS164 | |
A | GLN19 | |
A | CYS25 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
B | HIS164 | |
B | GLN19 | |
B | ASN184 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
A | HIS164 | |
A | GLN19 | |
A | ASN184 | |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
B | HIS164 | |
B | GLN19 | |
B | CYS25 | |
B | ASN184 | |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
A | HIS164 | |
A | GLN19 | |
A | CYS25 | |
A | ASN184 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 814 |
Chain | Residue | Details |
B | GLN19 | electrostatic stabiliser |
B | CYS25 | nucleofuge, nucleophile, proton acceptor, proton donor |
B | HIS164 | proton acceptor, proton donor |
B | ASN184 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 814 |
Chain | Residue | Details |
A | GLN19 | electrostatic stabiliser |
A | CYS25 | nucleofuge, nucleophile, proton acceptor, proton donor |
A | HIS164 | proton acceptor, proton donor |
A | ASN184 | electrostatic stabiliser |