5W3W
Crystal structure of SsoPox AsD6 mutant (V27A-Y97W-L228M-W263M) - open form
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 | HOH508 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CO A 402 |
Chain | Residue |
A | ARG223 |
A | FE2401 |
A | HOH508 |
A | KCX137 |
A | HIS170 |
A | HIS199 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | SER171 |
A | ASN172 |
A | ALA173 |
A | HIS174 |
A | ASP202 |
A | PHE229 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | ILE98 |
A | TYR99 |
A | ILE100 |
A | ASP101 |
D | EDO404 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | ASN160 |
A | LYS164 |
A | GLY189 |
A | ASP191 |
site_id | AC6 |
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 | HOH503 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue CO B 402 |
Chain | Residue |
B | KCX137 |
B | HIS170 |
B | HIS199 |
B | ARG223 |
B | FE2401 |
B | HOH503 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO B 403 |
Chain | Residue |
B | ILE98 |
B | TYR99 |
B | ILE100 |
B | ASP101 |
C | PHE104 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
B | ASN160 |
B | LYS164 |
B | GLY189 |
B | ASP191 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
B | GLY128 |
B | THR129 |
site_id | AD2 |
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 | HOH502 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue CO C 402 |
Chain | Residue |
C | KCX137 |
C | HIS170 |
C | HIS199 |
C | FE2401 |
C | HOH502 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue EDO C 403 |
Chain | Residue |
B | PHE104 |
C | TYR99 |
C | ASP101 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue GOL C 404 |
Chain | Residue |
C | ASN160 |
C | LYS164 |
C | GLY189 |
C | ASP191 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue EDO C 405 |
Chain | Residue |
C | GLY128 |
C | THR129 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue FE2 D 401 |
Chain | Residue |
D | HIS22 |
D | HIS24 |
D | KCX137 |
D | ASP256 |
D | CO402 |
D | GOL407 |
D | HOH503 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue CO D 402 |
Chain | Residue |
D | KCX137 |
D | HIS170 |
D | HIS199 |
D | ARG223 |
D | FE2401 |
D | HOH503 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue EDO D 403 |
Chain | Residue |
D | SER171 |
D | ASN172 |
D | ALA173 |
D | ASP202 |
D | PHE229 |
site_id | AE1 |
Number of Residues | 3 |
Details | binding site for residue EDO D 404 |
Chain | Residue |
A | EDO404 |
D | TYR99 |
D | ASP101 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue GOL D 405 |
Chain | Residue |
D | ASN160 |
D | LYS164 |
D | GLY189 |
D | ASP191 |
site_id | AE3 |
Number of Residues | 2 |
Details | binding site for residue EDO D 406 |
Chain | Residue |
D | GLY128 |
D | THR129 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue GOL D 407 |
Chain | Residue |
D | KCX137 |
D | FE2401 |
D | HIS24 |
D | ALA27 |
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 |
B | HIS199 | |
B | ASP256 | |
C | HIS22 | |
C | HIS24 | |
C | HIS170 | |
C | HIS199 | |
C | ASP256 | |
D | HIS22 | |
D | HIS24 | |
D | HIS170 | |
D | HIS199 | |
D | ASP256 | |
A | HIS170 | |
A | HIS199 | |
A | ASP256 | |
B | HIS22 | |
B | HIS24 | |
B | HIS170 | |
A | HIS22 | |
A | HIS24 |
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 |