13CU
Crystal structure of covalent inhibitor 2-chloro-N-(3-((pyridin-2-ylthio)methyl)phenyl)acetamide bound to Ubiquitin C-terminal Hydrolase-L3
This is a non-PDB format compatible entry.
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 | 30 |
| 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 | 3 |
| 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":"27941124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9790970","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| 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 | 3 |
| 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 | 3 |
| 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 | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by ATM","evidences":[{"source":"PubMed","id":"27941124","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| 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 |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 597 |
| Chain | Residue | Details |
| B | GLN89 | electrostatic stabiliser |
| B | CYS95 | covalent catalysis, proton shuttle (general acid/base) |
| B | HIS169 | proton shuttle (general acid/base) |
| B | ASP184 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 597 |
| Chain | Residue | Details |
| C | GLN89 | electrostatic stabiliser |
| C | CYS95 | covalent catalysis, proton shuttle (general acid/base) |
| C | HIS169 | proton shuttle (general acid/base) |
| C | ASP184 | electrostatic stabiliser |
