3C0R
Structure of Ovarian Tumor (OTU) domain in complex with Ubiquitin
Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0004843 | molecular_function | cysteine-type deubiquitinase activity | 
| A | 0016579 | biological_process | protein deubiquitination | 
| A | 0030433 | biological_process | ubiquitin-dependent ERAD pathway | 
| A | 0101005 | molecular_function | deubiquitinase activity | 
| C | 0004843 | molecular_function | cysteine-type deubiquitinase activity | 
| C | 0016579 | biological_process | protein deubiquitination | 
| C | 0030433 | biological_process | ubiquitin-dependent ERAD pathway | 
| C | 0101005 | molecular_function | deubiquitinase activity | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE 3CN B 76 | 
| Chain | Residue | 
| A | ASP116 | 
| A | ASP117 | 
| A | CYS120 | 
| A | TRP175 | 
| A | ILE221 | 
| A | HIS222 | 
| B | GLY75 | 
| site_id | AC2 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE 3CN D 76 | 
| Chain | Residue | 
| C | CYS120 | 
| C | TRP175 | 
| C | ILE221 | 
| C | HIS222 | 
| D | GLY75 | 
| C | ASP116 | 
| C | ASP117 | 
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 12 | 
| Details | Region: {"description":"Cys-loop","evidences":[{"source":"UniProtKB","id":"Q5VVQ6","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 8 | 
| Details | Region: {"description":"His-loop","evidences":[{"source":"UniProtKB","id":"Q5VVQ6","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 2 | 
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q96FW1","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 2 | 
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000305"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI5 | 
| Number of Residues | 2 | 
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q5VVQ6","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI6 | 
| Number of Residues | 2 | 
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q5VVQ6","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI7 | 
| Number of Residues | 4 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI8 | 
| Number of Residues | 4 | 
| Details | Site: {"description":"Interacts with activating enzyme"} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI9 | 
| Number of Residues | 2 | 
| Details | Site: {"description":"Essential for function"} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI10 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"PubMed","id":"24660806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24751536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24784582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25527291","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI11 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"(Microbial infection) ADP-ribosylthreonine","evidences":[{"source":"PubMed","id":"32330457","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI12 | 
| Number of Residues | 2 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI13 | 
| Number of Residues | 4 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719106","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI14 | 
| Number of Residues | 4 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI15 | 
| Number of Residues | 2 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"15466860","evidenceCode":"ECO:0000305"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI16 | 
| Number of Residues | 2 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34239127","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI17 | 
| Number of Residues | 2 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 











