4KET
Crystal structure of SsoPox W263I
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 | 7 |
Details | BINDING SITE FOR RESIDUE FE2 A 401 |
Chain | Residue |
A | HIS22 |
A | HIS24 |
A | KCX137 |
A | ASP256 |
A | CO402 |
A | EDO403 |
A | HOH699 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CO A 402 |
Chain | Residue |
A | HIS199 |
A | ARG223 |
A | FE2401 |
A | EDO403 |
A | HOH699 |
A | KCX137 |
A | HIS170 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO A 403 |
Chain | Residue |
A | HIS24 |
A | TYR97 |
A | KCX137 |
A | HIS170 |
A | ARG223 |
A | ASP256 |
A | FE2401 |
A | CO402 |
A | HOH699 |
A | HOH706 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 404 |
Chain | Residue |
A | PRO4 |
A | LEU5 |
A | LYS8 |
A | ASP9 |
A | SER10 |
A | LEU130 |
A | ASN131 |
A | LYS132 |
A | HOH552 |
A | HOH681 |
A | HOH694 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 405 |
Chain | Residue |
A | ASN160 |
A | LYS164 |
A | GLY189 |
A | VAL190 |
A | ASP191 |
A | HOH663 |
A | HOH676 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 406 |
Chain | Residue |
A | HIS120 |
A | GLU124 |
A | GLY128 |
A | THR129 |
A | HOH557 |
A | HOH581 |
A | HOH700 |
A | HOH711 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 407 |
Chain | Residue |
A | PHE104 |
C | TYR99 |
C | PG4404 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 401 |
Chain | Residue |
A | GLU298 |
A | HOH609 |
A | HOH683 |
B | GLN58 |
B | HOH576 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FE2 B 402 |
Chain | Residue |
B | HIS22 |
B | HIS24 |
B | KCX137 |
B | ASP256 |
B | CO403 |
B | GOL404 |
B | HOH718 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CO B 403 |
Chain | Residue |
B | KCX137 |
B | HIS170 |
B | HIS199 |
B | ARG223 |
B | FE2402 |
B | GOL404 |
B | HOH718 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 404 |
Chain | Residue |
B | HIS24 |
B | TYR97 |
B | KCX137 |
B | HIS170 |
B | ARG223 |
B | ASP256 |
B | FE2402 |
B | CO403 |
B | HOH718 |
site_id | BC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GOL B 405 |
Chain | Residue |
B | PRO4 |
B | LEU5 |
B | LYS8 |
B | ASP9 |
B | SER10 |
B | LEU130 |
B | ASN131 |
B | LYS132 |
B | HOH542 |
B | HOH685 |
B | HOH686 |
B | HOH722 |
B | HOH729 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 406 |
Chain | Residue |
B | LYS194 |
B | HOH636 |
B | ASN160 |
B | LYS164 |
B | GLY189 |
B | VAL190 |
B | ASP191 |
site_id | BC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PEG B 407 |
Chain | Residue |
B | HIS120 |
B | GLU124 |
B | GLY125 |
B | ILE126 |
B | GLN127 |
B | GLY128 |
B | THR129 |
B | LEU130 |
B | HOH589 |
B | HOH656 |
D | LYS164 |
D | HOH507 |
D | HOH703 |
site_id | BC6 |
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 | HOH688 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO C 402 |
Chain | Residue |
C | KCX137 |
C | HIS170 |
C | HIS199 |
C | FE2401 |
C | PG4404 |
C | HOH688 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 403 |
Chain | Residue |
C | ASP214 |
C | GLY246 |
C | TYR247 |
C | ASP249 |
site_id | BC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PG4 C 404 |
Chain | Residue |
A | EDO407 |
C | TYR97 |
C | HIS170 |
C | ARG223 |
C | LEU226 |
C | ASP256 |
C | TRP278 |
C | CO402 |
C | HOH688 |
C | HOH707 |
C | HOH712 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 405 |
Chain | Residue |
C | HIS120 |
C | GLU124 |
C | GLY128 |
C | THR129 |
C | HOH540 |
C | HOH550 |
site_id | CC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 406 |
Chain | Residue |
C | LEU102 |
C | PRO103 |
C | PHE104 |
C | LEU107 |
C | ASP148 |
C | HOH704 |
C | HOH706 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 407 |
Chain | Residue |
C | ASN160 |
C | LYS164 |
C | GLY189 |
C | ASP191 |
C | HOH599 |
site_id | CC4 |
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 | HOH701 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CO D 402 |
Chain | Residue |
D | KCX137 |
D | HIS170 |
D | HIS199 |
D | ARG223 |
D | FE2401 |
D | PG4404 |
D | HOH701 |
site_id | CC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO D 403 |
Chain | Residue |
C | ILE243 |
C | GLY295 |
C | VAL296 |
C | ASN297 |
C | VAL300 |
D | GLU12 |
D | LYS14 |
D | ASP15 |
D | HOH696 |
D | HOH719 |
site_id | CC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PG4 D 404 |
Chain | Residue |
D | TYR97 |
D | ARG223 |
D | ASP256 |
D | THR265 |
D | ALA266 |
D | ALA275 |
D | CO402 |
D | HOH701 |
D | HOH704 |
site_id | CC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL D 405 |
Chain | Residue |
D | ASP112 |
D | ASP116 |
D | ILE119 |
D | HOH710 |
D | HOH722 |
site_id | CC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 406 |
Chain | Residue |
D | GLN58 |
D | PHE59 |
D | HOH718 |
site_id | DC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL D 407 |
Chain | Residue |
D | ASN160 |
D | LYS164 |
D | GLY189 |
D | VAL190 |
D | ASP191 |
D | LYS194 |
D | HOH589 |
D | HOH706 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 408 |
Chain | Residue |
D | ASP249 |
D | LYS250 |
D | LYS311 |
D | HOH678 |
D | HOH702 |
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 | HIS22 | |
A | HIS24 | |
A | HIS170 | |
A | HIS199 | |
A | ASP256 | |
B | HIS22 | |
B | HIS24 | |
B | HIS170 |
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 |