8SFA
Crystal structure of the engineered SsoPox variant IIIC1
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 |
D | 0004063 | molecular_function | aryldialkylphosphatase activity |
D | 0008270 | molecular_function | zinc ion binding |
D | 0009056 | biological_process | catabolic process |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
D | 0046872 | molecular_function | metal ion binding |
S | 0004063 | molecular_function | aryldialkylphosphatase activity |
S | 0008270 | molecular_function | zinc ion binding |
S | 0009056 | biological_process | catabolic process |
S | 0016787 | molecular_function | hydrolase activity |
S | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
S | 0046872 | molecular_function | metal ion binding |
t | 0004063 | molecular_function | aryldialkylphosphatase activity |
t | 0008270 | molecular_function | zinc ion binding |
t | 0009056 | biological_process | catabolic process |
t | 0016787 | molecular_function | hydrolase activity |
t | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
t | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS01322 |
Number of Residues | 9 |
Details | PHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GfTLiHEHL |
Chain | Residue | Details |
D | GLY17-LEU25 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
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 |
D | HIS22 | |
S | ASP256 | |
b | HIS22 | |
b | HIS24 | |
b | HIS170 | |
b | HIS199 | |
b | ASP256 | |
t | HIS22 | |
t | HIS24 | |
t | HIS170 | |
t | HIS199 | |
D | HIS24 | |
t | ASP256 | |
D | HIS170 | |
D | HIS199 | |
D | ASP256 | |
S | HIS22 | |
S | HIS24 | |
S | HIS170 | |
S | HIS199 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
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 |
D | KCX137 | |
S | KCX137 | |
b | KCX137 | |
t | KCX137 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
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 |
D | KCX137 | |
S | KCX137 | |
b | KCX137 | |
t | KCX137 |