1Z0S
Crystal structure of an NAD kinase from Archaeoglobus fulgidus in complex with ATP
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 | 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 | 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 | 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 | 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 | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 5001 |
| Chain | Residue |
| A | ATP737 |
| A | POP3953 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 5002 |
| Chain | Residue |
| B | ATP738 |
| B | POP3954 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 5003 |
| Chain | Residue |
| C | ATP739 |
| C | POP3955 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 5004 |
| Chain | Residue |
| D | ATP740 |
| D | POP3956 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP A 737 |
| Chain | Residue |
| A | ARG54 |
| A | ASN115 |
| A | GLU116 |
| A | GLY157 |
| A | TYR158 |
| A | SER161 |
| A | ASP209 |
| A | GLN211 |
| A | POP3953 |
| A | MG5001 |
| A | HOH5030 |
| A | HOH5079 |
| D | ALA125 |
| D | LYS126 |
| D | MET127 |
| D | ARG143 |
| D | ASP145 |
| D | ALA180 |
| D | PHE182 |
| D | HOH5036 |
| A | GLY50 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP B 738 |
| Chain | Residue |
| B | GLY50 |
| B | ARG54 |
| B | ASN115 |
| B | GLU116 |
| B | GLY157 |
| B | TYR158 |
| B | SER161 |
| B | ASP209 |
| B | GLN211 |
| B | POP3954 |
| B | MG5002 |
| B | HOH5029 |
| C | ALA125 |
| C | LYS126 |
| C | MET127 |
| C | ARG143 |
| C | ASP145 |
| C | ALA180 |
| C | PHE182 |
| C | HOH5083 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP C 739 |
| Chain | Residue |
| B | ALA125 |
| B | LYS126 |
| B | MET127 |
| B | ARG143 |
| B | ASP145 |
| B | ALA180 |
| B | PHE182 |
| B | HOH5035 |
| C | GLY50 |
| C | ARG54 |
| C | ASN115 |
| C | GLU116 |
| C | GLY157 |
| C | TYR158 |
| C | SER161 |
| C | ASP209 |
| C | GLN211 |
| C | POP3955 |
| C | MG5003 |
| C | HOH5067 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP D 740 |
| Chain | Residue |
| A | ALA125 |
| A | LYS126 |
| A | MET127 |
| A | ARG143 |
| A | ASP145 |
| A | ALA180 |
| A | PHE182 |
| A | HOH5035 |
| D | GLY50 |
| D | ARG54 |
| D | ASN115 |
| D | GLU116 |
| D | GLY157 |
| D | TYR158 |
| D | SER161 |
| D | ASP209 |
| D | GLN211 |
| D | POP3956 |
| D | MG5004 |
| D | HOH5028 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE POP A 3953 |
| Chain | Residue |
| A | HOH5088 |
| A | LYS8 |
| A | GLY48 |
| A | GLY50 |
| A | THR51 |
| A | ARG54 |
| A | GLY71 |
| A | ARG72 |
| A | ATP737 |
| A | MG5001 |
| A | HOH5079 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE POP B 3954 |
| Chain | Residue |
| B | LYS8 |
| B | GLY48 |
| B | GLY50 |
| B | THR51 |
| B | ARG54 |
| B | ARG72 |
| B | ATP738 |
| B | MG5002 |
| B | HOH5062 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE POP C 3955 |
| Chain | Residue |
| C | LYS8 |
| C | GLY48 |
| C | ASP49 |
| C | GLY50 |
| C | THR51 |
| C | ARG54 |
| C | ARG72 |
| C | ATP739 |
| C | MG5003 |
| C | HOH5087 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE POP D 3956 |
| Chain | Residue |
| D | LYS8 |
| D | GLY48 |
| D | GLY50 |
| D | THR51 |
| D | ARG54 |
| D | ARG72 |
| D | ATP740 |
| D | MG5004 |
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 |
| C | ASP49 | |
| A | ASP49 | |
| B | 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 | |
| A | ARG143 | |
| A | ILE153 | |
| A | THR156 | |
| A | GLN211 | |
| B | ASP49 | |
| B | ARG54 | |
| B | ASN115 | |
| B | LYS126 | |
| B | ARG143 | |
| B | ILE153 | |
| B | THR156 | |
| B | GLN211 | |
| C | ASP49 | |
| C | ARG54 | |
| C | ASN115 | |
| C | LYS126 | |
| C | ARG143 | |
| C | ILE153 | |
| C | THR156 | |
| C | GLN211 | |
| D | ASP49 | |
| D | ARG54 | |
| D | ASN115 | |
| D | LYS126 | |
| D | ARG143 | |
| D | ILE153 | |
| D | THR156 | |
| D | GLN211 | |
| A | ARG54 | |
| A | ASN115 | |
| A | LYS126 |
| 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 |
