3H62
Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with cantharidic acid
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 500 |
| Chain | Residue |
| C | NHC0 |
| C | ASP271 |
| C | ASN303 |
| C | HIS352 |
| C | HIS427 |
| C | MN501 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 501 |
| Chain | Residue |
| C | ASP271 |
| C | MN500 |
| C | NHC0 |
| C | ASP242 |
| C | HIS244 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NHC C 0 |
| Chain | Residue |
| C | ASP242 |
| C | HIS244 |
| C | ASP271 |
| C | ARG275 |
| C | ASN303 |
| C | HIS304 |
| C | ARG400 |
| C | HIS427 |
| C | VAL429 |
| C | PHE446 |
| C | TYR451 |
| C | MN500 |
| C | MN501 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 500 |
| Chain | Residue |
| B | NHC0 |
| B | ASP271 |
| B | ASN303 |
| B | HIS352 |
| B | HIS427 |
| B | MN501 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 501 |
| Chain | Residue |
| B | NHC0 |
| B | ASP242 |
| B | HIS244 |
| B | ASP271 |
| B | MN500 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NHC B 0 |
| Chain | Residue |
| B | ASP242 |
| B | HIS244 |
| B | ASP271 |
| B | ARG275 |
| B | ASN303 |
| B | HIS304 |
| B | ARG400 |
| B | HIS427 |
| B | VAL429 |
| B | PHE446 |
| B | TYR451 |
| B | MN500 |
| B | MN501 |
| B | HOH690 |
Functional Information from PROSITE/UniProt
| site_id | PS00125 |
| Number of Residues | 6 |
| Details | SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE |
| Chain | Residue | Details |
| C | LEU300-GLU305 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15155720","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15155720","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15577939","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19601647","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S95","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WAO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H60","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H61","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H62","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H64","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15155720","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aui |
| Chain | Residue | Details |
| C | HIS304 | |
| C | ASP274 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aui |
| Chain | Residue | Details |
| B | HIS304 | |
| B | ASP274 |
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 472 |
| Chain | Residue | Details |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 472 |
| Chain | Residue | Details |
| B | ASP242 | metal ligand |
| B | HIS427 | activator, metal ligand |
| B | HIS244 | metal ligand |
| B | ASP271 | metal ligand |
| B | ASP274 | activator, proton donor |
| B | ARG275 | transition state stabiliser |
| B | ASN303 | metal ligand, transition state stabiliser |
| B | HIS304 | proton acceptor, proton donor, proton relay |
| B | HIS352 | metal ligand |
| B | ARG400 | transition state stabiliser |
