1SUW
Crystal structure of a NAD kinase from Archaeoglobus fulgidus in complex with its substrate and product: Insights into the catalysis of NAD kinase
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 | 0016310 | biological_process | phosphorylation |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| 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 | 0016310 | biological_process | phosphorylation |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| 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 | 0016310 | biological_process | phosphorylation |
| C | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| 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 | 0016310 | biological_process | phosphorylation |
| D | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| 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 | 23 |
| Details | BINDING SITE FOR RESIDUE NAP A 3075 |
| Chain | Residue |
| A | GLY48 |
| A | GLY157 |
| A | TYR158 |
| A | SER161 |
| A | ASP209 |
| A | GLY210 |
| A | GLN211 |
| A | HOH3082 |
| D | ALA125 |
| D | LYS126 |
| D | MET127 |
| A | ASP49 |
| D | ARG143 |
| D | ASP145 |
| D | ALA180 |
| D | PHE182 |
| A | GLY50 |
| A | ARG54 |
| A | VAL73 |
| A | ASN115 |
| A | GLU116 |
| A | ILE153 |
| A | THR156 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP B 3076 |
| Chain | Residue |
| B | GLY48 |
| B | ASP49 |
| B | GLY50 |
| B | LEU53 |
| B | ARG54 |
| B | VAL73 |
| B | LEU75 |
| B | ASN115 |
| B | GLU116 |
| B | ILE153 |
| B | THR156 |
| B | TYR158 |
| B | SER161 |
| B | ASP209 |
| B | GLY210 |
| B | GLN211 |
| B | HOH3079 |
| B | HOH3114 |
| B | HOH3134 |
| C | ALA125 |
| C | MET127 |
| C | ARG143 |
| C | ASP145 |
| C | ALA180 |
| C | PHE182 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAP C 3077 |
| Chain | Residue |
| B | ALA125 |
| B | LYS126 |
| B | MET127 |
| B | ARG143 |
| B | ASP145 |
| B | ALA180 |
| B | PHE182 |
| C | GLY48 |
| C | ASP49 |
| C | GLY50 |
| C | ARG54 |
| C | VAL73 |
| C | LEU75 |
| C | ASN115 |
| C | GLU116 |
| C | ILE153 |
| C | THR156 |
| C | GLY157 |
| C | TYR158 |
| C | SER161 |
| C | ASP209 |
| C | GLY210 |
| C | GLN211 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP D 3078 |
| Chain | Residue |
| A | ALA125 |
| A | MET127 |
| A | ARG143 |
| A | ASP145 |
| A | ALA180 |
| A | PHE182 |
| D | GLY48 |
| D | ASP49 |
| D | GLY50 |
| D | ARG54 |
| D | VAL73 |
| D | ASN115 |
| D | GLU116 |
| D | ILE153 |
| D | THR156 |
| D | GLY157 |
| D | TYR158 |
| D | SER161 |
| D | ASP209 |
| D | GLY210 |
| D | GLN211 |
| D | HOH3087 |
| D | HOH3099 |
| D | HOH3103 |
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 |
| Chain | Residue | Details |
| A | ASP49 | |
| B | ASP49 | |
| C | ASP49 | |
| D | ASP49 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:16242716 |
| Chain | Residue | Details |
| A | ASP49 | |
| B | ARG54 | |
| B | ASN115 | |
| B | LYS126 | |
| B | ARG143 | |
| B | ILE153 | |
| B | THR156 | |
| B | GLN211 | |
| C | ASP49 | |
| C | ARG54 | |
| C | ASN115 | |
| A | ARG54 | |
| C | LYS126 | |
| C | ARG143 | |
| C | ILE153 | |
| C | THR156 | |
| C | GLN211 | |
| D | ASP49 | |
| D | ARG54 | |
| D | ASN115 | |
| D | LYS126 | |
| D | ARG143 | |
| A | ASN115 | |
| D | ILE153 | |
| D | THR156 | |
| D | GLN211 | |
| A | LYS126 | |
| A | ARG143 | |
| A | ILE153 | |
| A | THR156 | |
| A | GLN211 | |
| B | ASP49 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16242716 |
| Chain | Residue | Details |
| A | ASP145 | |
| A | ALA180 | |
| B | ASP145 | |
| B | ALA180 | |
| C | ASP145 | |
| C | ALA180 | |
| D | ASP145 | |
| D | ALA180 |
