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: BINDING => ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL |
Chain | Residue | Details |
A | HIS55 | |
B | ASP301 | |
A | HIS57 | |
A | HIS201 | |
A | HIS230 | |
A | ASP301 | |
B | HIS55 | |
B | HIS57 | |
B | HIS201 | |
B | HIS230 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: via carbamate group => ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL |
Chain | Residue | Details |
A | LYS169 | |
B | LYS169 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-carboxylysine => ECO:0000255|PROSITE-ProRule:PRU00679, ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL |
Chain | Residue | Details |
A | LYS169 | |
B | LYS169 |
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 |