1EZ2
THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG DIISOPROPYLMETHYL PHOSPHONATE.
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 | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | HIS55 |
A | HIS57 |
A | KCX169 |
A | ASP301 |
A | ZN402 |
A | HOH1551 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 402 |
Chain | Residue |
A | ZN401 |
A | DII1403 |
A | HOH1551 |
A | KCX169 |
A | HIS201 |
A | HIS230 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | HIS55 |
B | HIS57 |
B | KCX169 |
B | ASP301 |
B | ZN402 |
B | HOH2609 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 402 |
Chain | Residue |
B | KCX169 |
B | HIS201 |
B | HIS230 |
B | ZN401 |
B | DII2403 |
B | HOH2609 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DII A 1403 |
Chain | Residue |
A | HIS57 |
A | TRP131 |
A | HIS201 |
A | SER308 |
A | ZN402 |
A | HOH1551 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DII B 2403 |
Chain | Residue |
B | TRP131 |
B | PHE132 |
B | HIS201 |
B | LEU271 |
B | ASP301 |
B | ZN402 |
B | HOH2609 |
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 | KCX169 | |
B | KCX169 |
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 | KCX169 | |
B | KCX169 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | a catalytic site defined by CSA, PubMed 15134445 |
Chain | Residue | Details |
A | ASP233 | |
A | HIS254 | |
A | ASP301 |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 159 |
Chain | Residue | Details |
A | HIS55 | metal ligand |
A | HIS57 | metal ligand |
A | KCX169 | 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 | KCX169 | 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 |