Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004063 | molecular_function | aryldialkylphosphatase activity |
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 | 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 FE2 A 401 |
Chain | Residue |
A | HIS22 |
A | HIS24 |
A | KCX137 |
A | ASP256 |
A | CO402 |
A | EDO407 |
A | HOH516 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CO A 402 |
Chain | Residue |
A | HIS199 |
A | FE2401 |
A | EDO407 |
A | HOH516 |
A | KCX137 |
A | HIS170 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | ASN160 |
A | LYS161 |
A | LYS164 |
A | GLY189 |
A | VAL190 |
A | ASP191 |
A | LYS194 |
A | HOH531 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | LYS161 |
A | GLU162 |
A | LYS164 |
A | HOH754 |
B | GLU162 |
B | LYS164 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | ASN172 |
A | ALA173 |
A | ASP202 |
A | ARG223 |
A | PHE229 |
A | HOH536 |
A | HOH544 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue GOL A 406 |
Chain | Residue |
A | ARG77 |
A | GLU80 |
A | THR129 |
A | HOH598 |
A | HOH735 |
B | ARG154 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue EDO A 407 |
Chain | Residue |
A | HIS24 |
A | TYR97 |
A | HIS170 |
A | ARG223 |
A | FE2401 |
A | CO402 |
A | HOH516 |
A | HOH519 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue FE2 B 401 |
Chain | Residue |
B | HIS22 |
B | HIS24 |
B | KCX137 |
B | ASP256 |
B | CO402 |
B | EDO408 |
B | HOH510 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue CO B 402 |
Chain | Residue |
B | KCX137 |
B | HIS170 |
B | HIS199 |
B | FE2401 |
B | EDO408 |
B | HOH510 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | ASN172 |
B | ALA173 |
B | HIS174 |
B | ASP202 |
B | PHE229 |
B | HOH528 |
B | HOH624 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
B | ALA173 |
B | HIS174 |
B | ASN175 |
B | ASN176 |
B | TYR208 |
site_id | AD3 |
Number of Residues | 11 |
Details | binding site for residue GOL B 405 |
Chain | Residue |
B | LEU39 |
B | TYR40 |
B | GLU45 |
B | THR260 |
B | ILE261 |
B | ASP262 |
B | HOH504 |
B | HOH508 |
B | HOH564 |
B | HOH579 |
B | HOH621 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue GOL B 406 |
Chain | Residue |
B | ALA213 |
B | ASP214 |
B | TYR247 |
B | ASP249 |
B | LYS250 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue GOL B 407 |
Chain | Residue |
B | ASN160 |
B | LYS164 |
B | GLY189 |
B | VAL190 |
B | ASP191 |
B | LYS194 |
B | HOH567 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for residue EDO B 408 |
Chain | Residue |
B | ARG223 |
B | FE2401 |
B | CO402 |
B | HOH510 |
B | HOH608 |
B | HIS24 |
B | TYR97 |
B | HIS170 |
Functional Information from PROSITE/UniProt
site_id | PS01322 |
Number of Residues | 9 |
Details | PHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GfTLiHEHL |
Chain | Residue | Details |
A | GLY17-LEU25 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18486146, ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7, ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER, ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET, ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV, ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1 |
Chain | Residue | Details |
A | ASP256 | |
B | HIS22 | |
B | HIS24 | |
B | HIS170 | |
B | HIS199 | |
B | ASP256 | |
A | HIS22 | |
A | HIS24 | |
A | HIS170 | |
A | HIS199 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: via carbamate group => ECO:0000269|PubMed:18486146, ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7, ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER, ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET, ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV, ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1 |
Chain | Residue | Details |
A | KCX137 | |
B | KCX137 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-carboxylysine => ECO:0000255|PROSITE-ProRule:PRU00679, ECO:0000269|PubMed:18486146, ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7, ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER, ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET, ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV, ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1 |
Chain | Residue | Details |
A | KCX137 | |
B | KCX137 | |