4KEZ
Crystal structure of SsoPox W263F
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 |
C | 0004063 | molecular_function | aryldialkylphosphatase activity |
C | 0008270 | molecular_function | zinc ion binding |
C | 0009056 | biological_process | catabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
C | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 A 401 |
Chain | Residue |
A | HIS22 |
A | HIS24 |
A | KCX137 |
A | ASP256 |
A | CO402 |
A | HOH773 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO A 402 |
Chain | Residue |
A | FE2401 |
A | HOH773 |
A | KCX137 |
A | HIS170 |
A | HIS199 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 403 |
Chain | Residue |
A | ASN160 |
A | LYS164 |
A | GLY189 |
A | VAL190 |
A | ASP191 |
A | LYS194 |
A | HOH639 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 404 |
Chain | Residue |
A | ASN172 |
A | ALA173 |
A | HIS174 |
A | ASP202 |
A | PHE229 |
A | HOH535 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 405 |
Chain | Residue |
A | PRO4 |
A | LEU5 |
A | LYS8 |
A | ASP9 |
A | SER10 |
A | LEU130 |
A | ASN131 |
A | LYS132 |
A | HOH533 |
A | HOH660 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 406 |
Chain | Residue |
A | LEU102 |
A | PRO103 |
A | PHE106 |
A | LEU107 |
A | ASP148 |
A | LYS151 |
A | HOH648 |
A | HOH679 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 B 401 |
Chain | Residue |
B | HIS22 |
B | HIS24 |
B | KCX137 |
B | ASP256 |
B | CO402 |
B | HOH755 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO B 402 |
Chain | Residue |
B | KCX137 |
B | HIS170 |
B | HIS199 |
B | FE2401 |
B | HOH755 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 403 |
Chain | Residue |
B | ASN160 |
B | LYS164 |
B | GLY189 |
B | VAL190 |
B | ASP191 |
B | LYS194 |
B | HOH617 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 404 |
Chain | Residue |
B | SER171 |
B | ASN172 |
B | ALA173 |
B | HIS174 |
B | ASP202 |
B | PHE229 |
B | HOH582 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 405 |
Chain | Residue |
B | PRO4 |
B | LEU5 |
B | LYS8 |
B | ASP9 |
B | SER10 |
B | ASN131 |
B | LYS132 |
B | HOH565 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 C 401 |
Chain | Residue |
C | HIS22 |
C | HIS24 |
C | KCX137 |
C | ASP256 |
C | CO402 |
C | HOH753 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO C 402 |
Chain | Residue |
C | KCX137 |
C | HIS170 |
C | HIS199 |
C | FE2401 |
C | EDO405 |
C | HOH753 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 403 |
Chain | Residue |
C | ASN160 |
C | LYS164 |
C | GLY189 |
C | VAL190 |
C | ASP191 |
C | HOH589 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 404 |
Chain | Residue |
C | HOH547 |
C | HOH578 |
C | SER171 |
C | ASN172 |
C | ALA173 |
C | HIS174 |
C | ASP202 |
C | PHE229 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 405 |
Chain | Residue |
C | TYR97 |
C | HIS170 |
C | ARG223 |
C | CO402 |
C | HOH663 |
C | HOH753 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 406 |
Chain | Residue |
C | ASP214 |
C | GLY246 |
C | TYR247 |
C | ASP249 |
C | LYS250 |
C | HOH677 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 D 401 |
Chain | Residue |
D | HIS22 |
D | HIS24 |
D | KCX137 |
D | ASP256 |
D | CO402 |
D | HOH759 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO D 402 |
Chain | Residue |
D | KCX137 |
D | HIS170 |
D | HIS199 |
D | FE2401 |
D | HOH759 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL D 403 |
Chain | Residue |
D | ASN160 |
D | LYS164 |
D | GLY189 |
D | ASP191 |
D | LYS194 |
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 | 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 |
A | HIS22 | |
B | ASP256 | |
C | HIS22 | |
C | HIS24 | |
C | HIS170 | |
C | HIS199 | |
C | ASP256 | |
D | HIS22 | |
D | HIS24 | |
D | HIS170 | |
D | HIS199 | |
A | HIS24 | |
D | ASP256 | |
A | HIS170 | |
A | HIS199 | |
A | ASP256 | |
B | HIS22 | |
B | HIS24 | |
B | HIS170 | |
B | 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 |
A | KCX137 | |
B | KCX137 | |
C | KCX137 | |
D | 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 |
A | KCX137 | |
B | KCX137 | |
C | KCX137 | |
D | KCX137 |