5EJG
Crystal structure of NAD kinase P252D mutant from Listeria monocytogenes
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0019674 | biological_process | NAD metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051287 | molecular_function | NAD 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 | 0019674 | biological_process | NAD metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD 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 | 0019674 | biological_process | NAD metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051287 | molecular_function | NAD 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 | 0019674 | biological_process | NAD metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780 |
| Chain | Residue | Details |
| A | ASP45 | |
| B | ASP45 | |
| C | ASP45 | |
| D | ASP45 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780 |
| Chain | Residue | Details |
| A | ASP45 | |
| B | SER158 | |
| B | THR161 | |
| B | HIS223 | |
| C | ASP45 | |
| C | GLY46 | |
| C | ASN122 | |
| C | SER158 | |
| C | THR161 | |
| C | HIS223 | |
| D | ASP45 | |
| A | GLY46 | |
| D | GLY46 | |
| D | ASN122 | |
| D | SER158 | |
| D | THR161 | |
| D | HIS223 | |
| A | ASN122 | |
| A | SER158 | |
| A | THR161 | |
| A | HIS223 | |
| B | ASP45 | |
| B | GLY46 | |
| B | ASN122 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361 |
| Chain | Residue | Details |
| A | ARG148 | |
| B | ARG148 | |
| C | ARG148 | |
| D | ARG148 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17686780 |
| Chain | Residue | Details |
| A | ASP150 | |
| B | ASP150 | |
| C | ASP150 | |
| D | ASP150 |
