7YV4
Crystal structure of human UCHL3 in complex with Farrerol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006508 | biological_process | proteolysis |
| A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| A | 0016567 | biological_process | protein ubiquitination |
| A | 0016579 | biological_process | protein deubiquitination |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019784 | molecular_function | deNEDDylase activity |
| A | 0030163 | biological_process | protein catabolic process |
| A | 0043130 | molecular_function | ubiquitin binding |
| A | 0043687 | biological_process | post-translational protein modification |
| A | 0101005 | molecular_function | deubiquitinase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00140 |
| Number of Residues | 17 |
| Details | UCH_1 Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site. QtisNACGtigLIHAIA |
| Chain | Residue | Details |
| A | GLN89-ALA105 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Region: {"description":"Interaction with ubiquitin","evidences":[{"source":"PubMed","id":"15531586","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19154770","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20380862","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9790970","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for enzyme activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 597 |
| Chain | Residue | Details |
| A | GLN89 | electrostatic stabiliser |
| A | CYS95 | covalent catalysis, proton shuttle (general acid/base) |
| A | HIS169 | proton shuttle (general acid/base) |
| A | ASP184 | electrostatic stabiliser |
