1NBF
Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| A | 0016579 | biological_process | protein deubiquitination |
| B | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| B | 0016579 | biological_process | protein deubiquitination |
| E | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| E | 0016579 | biological_process | protein deubiquitination |
Functional Information from PROSITE/UniProt
| site_id | PS00299 |
| Number of Residues | 26 |
| Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
| Chain | Residue | Details |
| C | LYS327-ASP352 |
| 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 | 614 |
| Details | Domain: {"description":"USP"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| 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_FI3 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12507430","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12507430 |
| Chain | Residue | Details |
| A | ASN218 | |
| A | CYS223 | |
| A | CYS223 | |
| A | ASP481 | |
| A | HIS464 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12507430 |
| Chain | Residue | Details |
| B | ASN218 | |
| B | CYS223 | |
| B | CYS223 | |
| B | ASP481 | |
| B | HIS464 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12507430 |
| Chain | Residue | Details |
| E | ASN218 | |
| E | CYS223 | |
| E | CYS223 | |
| E | ASP481 | |
| E | HIS464 |
| 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 |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 789 |
| Chain | Residue | Details |
| E | ASN218 | electrostatic stabiliser |
| E | CYS223 | nucleofuge, nucleophile, proton acceptor, proton donor |
| E | HIS464 | proton acceptor, proton donor |
| E | ASP481 | electrostatic stabiliser |
