1I0D
HIGH RESOLUTION STRUCTURE OF THE ZINC/CADMIUM-CONTAINING PHOSPHOTRIESTERASE FROM PSEUDOMONAS DIMINUTA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004063 | molecular_function | aryldialkylphosphatase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009056 | biological_process | catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004063 | molecular_function | aryldialkylphosphatase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009056 | biological_process | catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | ASP301 |
| A | FMT369 |
| A | CD402 |
| A | EDO406 |
| A | HOH1054 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CD A 402 |
| Chain | Residue |
| A | FMT369 |
| A | ZN401 |
| A | HOH876 |
| A | HOH1054 |
| A | HOH1056 |
| A | HIS201 |
| A | HIS230 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS55 |
| B | HIS57 |
| B | ASP301 |
| B | FMT369 |
| B | CD402 |
| B | EDO405 |
| B | HOH1053 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CD B 402 |
| Chain | Residue |
| B | HIS201 |
| B | HIS230 |
| B | FMT369 |
| B | ZN401 |
| B | HOH1053 |
| B | HOH1055 |
| B | HOH1059 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 403 |
| Chain | Residue |
| A | ASN38 |
| A | ILE154 |
| A | HOH796 |
| A | HOH1058 |
| A | HOH1063 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 404 |
| Chain | Residue |
| B | ASN38 |
| B | ILE154 |
| B | HOH794 |
| B | HOH818 |
| B | HOH1062 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 405 |
| Chain | Residue |
| B | HIS57 |
| B | TRP131 |
| B | ASP301 |
| B | FMT369 |
| B | ZN401 |
| B | EDO420 |
| B | HOH524 |
| B | HOH1053 |
| B | HOH1055 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 406 |
| Chain | Residue |
| A | HIS57 |
| A | ILE106 |
| A | TRP131 |
| A | FMT369 |
| A | ZN401 |
| A | EDO421 |
| A | HOH1054 |
| A | HOH1056 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 407 |
| Chain | Residue |
| A | ARG91 |
| B | THR147 |
| B | HOH715 |
| B | HOH795 |
| B | HOH1129 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 408 |
| Chain | Residue |
| A | HOH802 |
| A | HOH1057 |
| A | HOH1066 |
| A | HOH1087 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 409 |
| Chain | Residue |
| A | GLU81 |
| A | VAL84 |
| A | GLU115 |
| A | ALA119 |
| A | HOH488 |
| A | HOH823 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 410 |
| Chain | Residue |
| A | THR147 |
| A | ARG189 |
| A | EDO411 |
| A | HOH555 |
| A | HOH792 |
| A | HOH1060 |
| B | ARG91 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 411 |
| Chain | Residue |
| A | EDO410 |
| B | ARG91 |
| B | ASP121 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 412 |
| Chain | Residue |
| B | LYS77 |
| B | ALA80 |
| B | GLU115 |
| B | GLU344 |
| B | HOH1116 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 413 |
| Chain | Residue |
| B | PRO256 |
| B | TRP277 |
| B | VAL320 |
| B | PHE327 |
| B | HOH798 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEL B 414 |
| Chain | Residue |
| B | LYS77 |
| B | MET293 |
| B | LYS294 |
| B | GLY348 |
| B | ASN353 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEL A 415 |
| Chain | Residue |
| A | ILE349 |
| A | ASN353 |
| A | HOH890 |
| A | LYS77 |
| A | MET293 |
| A | THR345 |
| A | GLY348 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO A 416 |
| Chain | Residue |
| A | ASP133 |
| A | PRO134 |
| A | PRO135 |
| A | HOH459 |
| A | HOH460 |
| A | HOH462 |
| B | ASP133 |
| B | PRO134 |
| B | PRO135 |
| B | HOH521 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 417 |
| Chain | Residue |
| A | SER47 |
| A | GLU48 |
| A | ARG96 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 418 |
| Chain | Residue |
| B | SER47 |
| B | GLU48 |
| B | GLY50 |
| B | ARG96 |
| B | HIS123 |
| B | HOH639 |
| B | HOH1030 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 419 |
| Chain | Residue |
| A | ARG41 |
| A | GLY42 |
| A | PRO43 |
| B | GLU338 |
| B | HOH803 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 420 |
| Chain | Residue |
| B | HIS257 |
| B | ASP301 |
| B | LEU303 |
| B | EDO405 |
| B | HOH1053 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 421 |
| Chain | Residue |
| A | PHE306 |
| A | SER308 |
| A | TYR309 |
| A | EDO406 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT A 369 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | LYS169 |
| A | HIS201 |
| A | HIS230 |
| A | ZN401 |
| A | CD402 |
| A | EDO406 |
| A | HOH1054 |
| site_id | CC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT B 369 |
| Chain | Residue |
| B | HIS55 |
| B | HIS57 |
| B | LYS169 |
| B | HIS201 |
| B | HIS230 |
| B | ZN401 |
| B | CD402 |
| B | EDO405 |
| B | HOH1053 |
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 |
