2AKO
Crystal structure of Glutamate 5-kinase from Campylobacter jejuni
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004349 | molecular_function | glutamate 5-kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0055129 | biological_process | L-proline biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004349 | molecular_function | glutamate 5-kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0055129 | biological_process | L-proline biosynthetic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004349 | molecular_function | glutamate 5-kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0055129 | biological_process | L-proline biosynthetic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004349 | molecular_function | glutamate 5-kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP A 852 |
| Chain | Residue |
| A | HIS11 |
| A | PRO172 |
| A | SER173 |
| A | THR204 |
| A | GLY206 |
| A | ILE207 |
| A | LYS210 |
| A | HOH891 |
| A | HOH1009 |
| A | HOH1017 |
| A | HOH1026 |
| A | SER162 |
| A | HOH1039 |
| A | HOH1040 |
| A | ASP163 |
| A | ILE164 |
| A | GLY166 |
| A | PHE167 |
| A | TYR168 |
| A | LYS170 |
| A | ASN171 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADP B 853 |
| Chain | Residue |
| B | HIS11 |
| B | SER162 |
| B | ASP163 |
| B | ILE164 |
| B | GLY166 |
| B | PHE167 |
| B | TYR168 |
| B | ASN171 |
| B | SER173 |
| B | THR204 |
| B | GLY206 |
| B | ILE207 |
| B | LYS210 |
| B | HOH864 |
| B | HOH868 |
| B | HOH900 |
| B | HOH965 |
| B | HOH968 |
| B | HOH986 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP C 854 |
| Chain | Residue |
| C | HIS11 |
| C | SER162 |
| C | ASP163 |
| C | ILE164 |
| C | GLY166 |
| C | PHE167 |
| C | TYR168 |
| C | LYS170 |
| C | ASN171 |
| C | SER173 |
| C | THR204 |
| C | GLY206 |
| C | ILE207 |
| C | LYS210 |
| C | HOH864 |
| C | HOH926 |
| C | HOH958 |
| C | HOH959 |
| C | HOH997 |
| C | HOH1001 |
| C | HOH1016 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADP D 855 |
| Chain | Residue |
| D | HIS11 |
| D | ASP141 |
| D | SER162 |
| D | ASP163 |
| D | ILE164 |
| D | GLY166 |
| D | PHE167 |
| D | TYR168 |
| D | ASN171 |
| D | PRO172 |
| D | SER173 |
| D | THR204 |
| D | GLY206 |
| D | ILE207 |
| D | LYS210 |
| D | HOH888 |
| D | HOH895 |
| D | HOH976 |
| D | HOH998 |
Functional Information from PROSITE/UniProt
| site_id | PS00902 |
| Number of Residues | 18 |
| Details | GLUTAMATE_5_KINASE Glutamate 5-kinase signature. SehGtGGIvTKLkAAkfL |
| Chain | Residue | Details |
| A | SER200-LEU217 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00456","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | Binding site: {} |
| Chain | Residue | Details |
