5DHP
Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with a novel inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003951 | molecular_function | NAD+ kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006741 | biological_process | NADP+ biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019674 | biological_process | NAD+ metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003951 | molecular_function | NAD+ kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006741 | biological_process | NADP+ biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019674 | biological_process | NAD+ metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003951 | molecular_function | NAD+ kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006741 | biological_process | NADP+ biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019674 | biological_process | NAD+ metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003951 | molecular_function | NAD+ kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006741 | biological_process | NADP+ biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0019674 | biological_process | NAD+ metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue CIT A 301 |
| Chain | Residue |
| A | VAL98 |
| A | TYR100 |
| A | HIS173 |
| A | PHE251 |
| A | PRO252 |
| A | PHE253 |
| A | ARG256 |
| A | HOH401 |
| A | HOH404 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | LYS127 |
| A | ASP150 |
| A | MET184 |
| C | ASP150 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue 5AQ A 303 |
| Chain | Residue |
| A | ASN122 |
| A | GLU123 |
| A | ALA162 |
| A | TYR163 |
| A | SER166 |
| A | HIS223 |
| A | HOH468 |
| C | GLY131 |
| C | PRO132 |
| C | GLY149 |
| C | ASP150 |
| C | ALA185 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue CIT B 301 |
| Chain | Residue |
| B | VAL98 |
| B | TYR100 |
| B | HIS173 |
| B | ARG247 |
| B | PRO252 |
| B | PHE253 |
| B | ARG256 |
| B | HOH401 |
| B | HOH404 |
| B | HOH407 |
| B | HOH431 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue 5AQ B 302 |
| Chain | Residue |
| B | ASN122 |
| B | GLU123 |
| B | ALA162 |
| B | TYR163 |
| B | SER166 |
| B | ASP222 |
| B | HIS223 |
| B | HOH433 |
| D | GLY131 |
| D | PRO132 |
| D | GLY149 |
| D | ASP150 |
| D | ALA185 |
| D | ILE187 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue 5AQ C 301 |
| Chain | Residue |
| A | GLY131 |
| A | PRO132 |
| A | GLY149 |
| A | ASP150 |
| A | ALA185 |
| C | ASN122 |
| C | GLU123 |
| C | ALA162 |
| C | TYR163 |
| C | SER166 |
| C | ASP222 |
| C | HOH437 |
| C | HOH438 |
| C | HOH447 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CIT D 301 |
| Chain | Residue |
| D | TYR100 |
| D | HIS173 |
| D | ARG247 |
| D | PHE251 |
| D | PRO252 |
| D | PHE253 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue 5AQ D 302 |
| Chain | Residue |
| B | ARG148 |
| B | ASP150 |
| B | ALA185 |
| B | ILE187 |
| D | ASN122 |
| D | GLU123 |
| D | ALA162 |
| D | TYR163 |
| D | SER166 |
| D | HIS223 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00361","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17686780","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00361","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17686780","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00361","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17686780","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
