3CS2
Crystal structure of PTE G60A mutant
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 |
K | 0004063 | molecular_function | aryldialkylphosphatase activity |
K | 0005886 | cellular_component | plasma membrane |
K | 0008270 | molecular_function | zinc ion binding |
K | 0009056 | biological_process | catabolic process |
K | 0016787 | molecular_function | hydrolase activity |
K | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
K | 0046872 | molecular_function | metal ion binding |
P | 0004063 | molecular_function | aryldialkylphosphatase activity |
P | 0005886 | cellular_component | plasma membrane |
P | 0008270 | molecular_function | zinc ion binding |
P | 0009056 | biological_process | catabolic process |
P | 0016787 | molecular_function | hydrolase activity |
P | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
P | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CAC A 1 |
Chain | Residue |
A | HIS57 |
A | ILE106 |
A | TRP131 |
A | HIS201 |
A | ASP301 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CAC B 2 |
Chain | Residue |
B | ASP301 |
B | HIS57 |
B | ILE106 |
B | TRP131 |
B | HIS201 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CAC K 3 |
Chain | Residue |
K | HIS57 |
K | ILE106 |
K | TRP131 |
K | HIS201 |
K | ASP301 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CAC P 4 |
Chain | Residue |
P | HIS57 |
P | ILE106 |
P | TRP131 |
P | HIS201 |
P | ASP301 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CO A 365 |
Chain | Residue |
A | HIS55 |
A | HIS57 |
A | ASP301 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CO A 2 |
Chain | Residue |
A | HIS201 |
A | HIS230 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CO B 3 |
Chain | Residue |
B | HIS55 |
B | HIS57 |
B | ASP301 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CO B 4 |
Chain | Residue |
B | HIS201 |
B | HIS230 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CO K 5 |
Chain | Residue |
K | HIS55 |
K | HIS57 |
K | ASP301 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CO K 6 |
Chain | Residue |
K | HIS201 |
K | HIS230 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CO P 7 |
Chain | Residue |
P | HIS55 |
P | HIS57 |
P | ASP301 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CO P 8 |
Chain | Residue |
P | HIS201 |
P | HIS230 |
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 | 20 |
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 | |
K | HIS55 | |
K | HIS57 | |
K | HIS201 | |
K | HIS230 | |
K | ASP301 | |
P | HIS55 | |
P | HIS57 | |
P | HIS201 | |
P | HIS230 | |
A | HIS57 | |
P | ASP301 | |
A | HIS201 | |
A | HIS230 | |
A | ASP301 | |
B | HIS55 | |
B | HIS57 | |
B | HIS201 | |
B | HIS230 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
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 | |
K | KCX169 | |
P | KCX169 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
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 | |
K | KCX169 | |
P | KCX169 |
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 | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ez2 |
Chain | Residue | Details |
K | HIS254 | |
K | ASP233 | |
K | ASP301 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ez2 |
Chain | Residue | Details |
P | HIS254 | |
P | ASP233 | |
P | 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 |
site_id | MCSA3 |
Number of Residues | 8 |
Details | M-CSA 159 |
Chain | Residue | Details |
K | HIS55 | metal ligand |
K | HIS57 | metal ligand |
K | KCX169 | metal ligand |
K | HIS201 | metal ligand |
K | HIS230 | metal ligand |
K | ASP233 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
K | HIS254 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
K | ASP301 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 8 |
Details | M-CSA 159 |
Chain | Residue | Details |
P | HIS55 | metal ligand |
P | HIS57 | metal ligand |
P | KCX169 | metal ligand |
P | HIS201 | metal ligand |
P | HIS230 | metal ligand |
P | ASP233 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
P | HIS254 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
P | ASP301 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |