1HZY
HIGH RESOLUTION STRUCTURE OF THE ZINC-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 | ZN402 |
| A | EDO408 |
| A | HOH876 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | FMT369 |
| A | ZN401 |
| A | HOH876 |
| A | HOH897 |
| 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 | ZN402 |
| B | EDO407 |
| B | HOH831 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| B | HIS201 |
| B | HIS230 |
| B | FMT369 |
| B | ZN401 |
| B | HOH831 |
| B | HOH919 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 405 |
| Chain | Residue |
| A | ASN38 |
| A | ILE154 |
| A | HOH436 |
| A | HOH815 |
| A | HOH963 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 406 |
| Chain | Residue |
| B | ASN38 |
| B | ILE154 |
| B | HOH635 |
| B | HOH812 |
| B | HOH873 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 407 |
| Chain | Residue |
| B | HIS57 |
| B | ILE106 |
| B | TRP131 |
| B | FMT369 |
| B | ZN401 |
| B | EDO422 |
| B | EDO423 |
| B | HOH919 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 408 |
| Chain | Residue |
| A | HIS57 |
| A | ILE106 |
| A | TRP131 |
| A | PHE306 |
| A | FMT369 |
| A | ZN401 |
| A | EDO425 |
| A | EDO426 |
| A | HOH897 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 409 |
| Chain | Residue |
| A | ARG91 |
| B | THR147 |
| B | HOH722 |
| B | HOH813 |
| B | HOH1060 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 410 |
| Chain | Residue |
| A | LEU182 |
| A | HOH541 |
| A | HOH838 |
| A | HOH853 |
| A | HOH1177 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 411 |
| Chain | Residue |
| A | GLU115 |
| A | HOH498 |
| A | HOH890 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 412 |
| Chain | Residue |
| A | THR147 |
| A | ARG189 |
| A | HOH563 |
| A | HOH808 |
| A | HOH906 |
| B | ARG91 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 413 |
| Chain | Residue |
| B | ARG76 |
| B | GLU115 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 414 |
| Chain | Residue |
| B | GLY305 |
| B | PHE306 |
| B | MET314 |
| B | HOH779 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 415 |
| Chain | Residue |
| B | PRO256 |
| B | TRP277 |
| B | VAL320 |
| B | PHE327 |
| B | HOH825 |
| B | HOH1178 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 416 |
| Chain | Residue |
| A | ASP133 |
| A | PRO134 |
| A | PRO135 |
| A | HOH469 |
| A | HOH472 |
| A | HOH537 |
| B | ASP133 |
| B | PRO134 |
| B | PRO135 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 417 |
| Chain | Residue |
| A | VAL351 |
| A | HOH450 |
| A | HOH993 |
| A | HOH1119 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 418 |
| Chain | Residue |
| A | ALA270 |
| A | ALA266 |
| A | SER269 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 419 |
| Chain | Residue |
| A | SER276 |
| A | THR279 |
| A | HOH594 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 420 |
| Chain | Residue |
| A | PRO256 |
| A | TRP277 |
| A | VAL320 |
| A | PHE327 |
| A | HOH877 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 421 |
| Chain | Residue |
| B | TRP131 |
| B | PHE132 |
| B | PRO134 |
| B | THR177 |
| B | GLN180 |
| B | HOH700 |
| B | HOH702 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 422 |
| Chain | Residue |
| B | SER308 |
| B | TYR309 |
| B | EDO407 |
| B | HOH920 |
| B | HOH1191 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 423 |
| Chain | Residue |
| B | HIS257 |
| B | ASP301 |
| B | EDO407 |
| B | HOH831 |
| B | HOH1124 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 424 |
| Chain | Residue |
| A | HOH1120 |
| B | SER47 |
| B | GLU48 |
| B | GLY50 |
| B | ARG96 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 425 |
| Chain | Residue |
| A | HIS254 |
| A | HIS257 |
| A | ASP301 |
| A | EDO408 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 426 |
| Chain | Residue |
| A | SER308 |
| A | TYR309 |
| A | EDO408 |
| A | HOH1190 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEL B 427 |
| Chain | Residue |
| B | LYS77 |
| B | MET293 |
| B | THR345 |
| B | GLY348 |
| B | ASN353 |
| site_id | DC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEL A 428 |
| Chain | Residue |
| A | LYS77 |
| A | MET293 |
| A | LYS294 |
| A | THR345 |
| A | GLY348 |
| A | ILE349 |
| A | ASN353 |
| site_id | DC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FMT A 369 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | ILE106 |
| A | LYS169 |
| A | HIS201 |
| A | HIS230 |
| A | ZN401 |
| A | ZN402 |
| A | EDO408 |
| A | HOH876 |
| site_id | DC3 |
| 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 | ZN402 |
| B | EDO407 |
| B | HOH831 |
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 |
