6ISU
Crystal structure of Lys27-linked di-ubiquitin in complex with its selective interacting protein UCHL3
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 |
site_id | PS00299 |
Number of Residues | 26 |
Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
Chain | Residue | Details |
C | SLZ27-ASP52 | |
B | LYS27-ASP52 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 224 |
Details | Domain: {"description":"UCH catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | Region: {"description":"Interaction with ubiquitin","evidences":[{"source":"PubMed","id":"15531586","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
Details | Region: {"description":"Interaction with ubiquitin. Crossover loop which restricts access of large ubiquitin adducts to the active site","evidences":[{"source":"PubMed","id":"15531586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19047059","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
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_FI5 |
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_FI6 |
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_FI7 |
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_FI8 |
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 |
site_id | SWS_FT_FI9 |
Number of Residues | 75 |
Details | Domain: {"description":"Ubiquitin-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]} |
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 |