1PSC
PHOSPHOTRIESTERASE FROM PSEUDOMONAS DIMINUTA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009056 | biological_process | catabolic process |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009056 | biological_process | catabolic process |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD A 801 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | ASP301 |
| A | FMT901 |
| A | HOH912 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CD A 802 |
| Chain | Residue |
| A | HOH912 |
| A | HOH985 |
| A | HIS201 |
| A | HIS230 |
| A | FMT901 |
| A | HOH905 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD B 803 |
| Chain | Residue |
| B | HIS55 |
| B | HIS57 |
| B | ASP301 |
| B | FMT902 |
| B | HOH1004 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CD B 804 |
| Chain | Residue |
| B | HIS201 |
| B | HIS230 |
| B | FMT902 |
| B | HOH1002 |
| B | HOH1003 |
| B | HOH1004 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EBP A 900 |
| Chain | Residue |
| A | PHE51 |
| A | GLU71 |
| B | LEU151 |
| B | ARG152 |
| B | GLN155 |
| B | TYR156 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EBP B 901 |
| Chain | Residue |
| A | LEU151 |
| A | ARG152 |
| A | GLN155 |
| A | TYR156 |
| B | PHE51 |
| B | HOH1038 |
| B | HOH1105 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A 901 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | LYS169 |
| A | HIS201 |
| A | HIS230 |
| A | CD801 |
| A | CD802 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT B 902 |
| Chain | Residue |
| B | HIS55 |
| B | HIS57 |
| B | LYS169 |
| B | HIS201 |
| B | HIS230 |
| B | CD803 |
| B | CD804 |
Functional Information from PROSITE/UniProt
| site_id | PS01322 |
| Number of Residues | 9 |
| Details | PHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GfTLtHEHI |
| Chain | Residue | Details |
| A | GLY50-ILE58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00679","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ez2 |
| Chain | Residue | Details |
| A | HIS254 | |
| A | ASP233 | |
| A | ASP301 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ez2 |
| Chain | Residue | Details |
| B | HIS254 | |
| B | ASP233 | |
| B | ASP301 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 159 |
| Chain | Residue | Details |
| A | HIS55 | metal ligand |
| A | HIS57 | metal ligand |
| A | LYS169 | metal ligand |
| A | HIS201 | metal ligand |
| A | HIS230 | metal ligand |
| A | ASP233 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS254 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | ASP301 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 159 |
| Chain | Residue | Details |
| B | HIS55 | metal ligand |
| B | HIS57 | metal ligand |
| B | LYS169 | metal ligand |
| B | HIS201 | metal ligand |
| B | HIS230 | metal ligand |
| B | ASP233 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS254 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | ASP301 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
