4C5N
Structure of the pyridoxal kinase from Staphylococcus aureus in complex with AMP-PCP and pyridoxal
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
A | 0009228 | biological_process | thiamine biosynthetic process |
B | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
B | 0009228 | biological_process | thiamine biosynthetic process |
C | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
C | 0009228 | biological_process | thiamine biosynthetic process |
D | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
D | 0009228 | biological_process | thiamine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PXL A 300 |
Chain | Residue |
A | GLY11 |
A | SER12 |
A | ASP13 |
A | GLY19 |
A | CYS214 |
A | ACP500 |
A | HOH2007 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ACP A 500 |
Chain | Residue |
A | ASP188 |
A | ASP202 |
A | MET203 |
A | PHE204 |
A | GLN205 |
A | ASN209 |
A | HIS210 |
A | GLY211 |
A | ALA212 |
A | GLY213 |
A | CYS214 |
A | LYS238 |
A | ILE245 |
A | PXL300 |
A | HOH2051 |
A | HOH2056 |
A | LYS176 |
A | SER186 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PXL B 300 |
Chain | Residue |
B | GLY11 |
B | SER12 |
B | ASP13 |
B | GLY19 |
B | VAL42 |
B | MET80 |
B | VAL107 |
B | HIS210 |
B | CYS214 |
B | ACP500 |
B | HOH2005 |
site_id | AC4 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ACP B 500 |
Chain | Residue |
B | LYS176 |
B | GLY178 |
B | SER186 |
B | ASP188 |
B | ASP202 |
B | MET203 |
B | PHE204 |
B | GLN205 |
B | GLN206 |
B | ASN209 |
B | HIS210 |
B | GLY211 |
B | ALA212 |
B | GLY213 |
B | CYS214 |
B | LYS238 |
B | ILE245 |
B | PXL300 |
B | HOH2053 |
B | HOH2054 |
B | HOH2062 |
B | HOH2085 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PXL C 300 |
Chain | Residue |
C | GLY11 |
C | GLY19 |
C | CYS214 |
C | ACP500 |
C | HOH2009 |
site_id | AC6 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ACP C 500 |
Chain | Residue |
C | LYS176 |
C | GLY178 |
C | LYS179 |
C | SER186 |
C | ASP188 |
C | ASP202 |
C | MET203 |
C | PHE204 |
C | GLN205 |
C | ASN209 |
C | HIS210 |
C | GLY211 |
C | ALA212 |
C | GLY213 |
C | CYS214 |
C | LYS238 |
C | ILE245 |
C | PXL300 |
C | HOH2047 |
C | HOH2048 |
C | HOH2058 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE UEG D 300 |
Chain | Residue |
D | GLY11 |
D | GLY19 |
D | VAL42 |
D | VAL109 |
D | CYS110 |
D | HIS210 |
D | CYS214 |
D | HOH2003 |
D | HOH2016 |
site_id | AC8 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ACP D 500 |
Chain | Residue |
D | PHE204 |
D | GLN205 |
D | ASN209 |
D | GLY211 |
D | ALA212 |
D | GLY213 |
D | CYS214 |
D | LYS238 |
D | ILE245 |
D | HOH2035 |
D | HOH2036 |
D | ASN139 |
D | LYS176 |
D | GLY178 |
D | SER186 |
D | ASP188 |
D | ASP202 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 1277 |
Chain | Residue |
C | GLN205 |
C | GLN206 |
C | SER207 |
D | THR274 |
D | GLU275 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 D 1277 |
Chain | Residue |
D | GLN206 |
D | SER207 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 1278 |
Chain | Residue |
D | GLY72 |
D | ASN98 |
D | HOH2019 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 1279 |
Chain | Residue |
D | LEU30 |
D | TYR223 |
D | TYR263 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 1277 |
Chain | Residue |
B | GLY72 |
B | ASN98 |
B | HOH2038 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 1278 |
Chain | Residue |
A | LYS185 |
B | HIS172 |
B | HOH2074 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 1278 |
Chain | Residue |
C | GLY72 |
C | ASN98 |
C | HOH2008 |