5VSK
Structure of DUB complex
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue 9HS A 601 |
| Chain | Residue |
| A | TYR224 |
| A | HIS456 |
| A | TYR465 |
| A | TYR514 |
| A | ASP295 |
| A | VAL296 |
| A | GLN297 |
| A | GLN405 |
| A | MET407 |
| A | ARG408 |
| A | PHE409 |
| A | LYS420 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 602 |
| Chain | Residue |
| A | CYS300 |
| A | ASP349 |
| A | HIS403 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 603 |
| Chain | Residue |
| A | HIS464 |
| A | ASP481 |
| B | ASP459 |
| B | HIS461 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue 9HS B 601 |
| Chain | Residue |
| B | TYR224 |
| B | ASP295 |
| B | VAL296 |
| B | GLN297 |
| B | LEU406 |
| B | MET407 |
| B | ARG408 |
| B | PHE409 |
| B | LYS420 |
| B | HIS456 |
| B | HIS461 |
| B | TYR465 |
| B | TYR514 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 602 |
| Chain | Residue |
| B | CYS300 |
| B | HIS403 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 603 |
| Chain | Residue |
| A | ASP459 |
| A | HIS461 |
| B | HIS464 |
| B | ASP481 |
Functional Information from PROSITE/UniProt
| site_id | PS00972 |
| Number of Residues | 16 |
| Details | USP_1 Ubiquitin specific protease (USP) domain signature 1. GLknqGAtCYMNSlLQ |
| Chain | Residue | Details |
| A | GLY215-GLN230 |
| site_id | PS00973 |
| Number of Residues | 18 |
| Details | USP_2 Ubiquitin specific protease (USP) domain signature 2. YiLhAVlvHsGdnhg..GHY |
| Chain | Residue | Details |
| A | TYR448-TYR465 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12507430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25944111","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11923872","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15053880","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16964248","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18716620","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21745816","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22411829","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12507430","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 789 |
| Chain | Residue | Details |
| A | ASN218 | electrostatic stabiliser |
| A | CYS223 | nucleofuge, nucleophile, proton acceptor, proton donor |
| A | HIS464 | proton acceptor, proton donor |
| A | ASP481 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 789 |
| Chain | Residue | Details |
| B | ASN218 | electrostatic stabiliser |
| B | CYS223 | nucleofuge, nucleophile, proton acceptor, proton donor |
| B | HIS464 | proton acceptor, proton donor |
| B | ASP481 | electrostatic stabiliser |
