1F9A
CRYSTAL STRUCTURE ANALYSIS OF NMN ADENYLYLTRANSFERASE FROM METHANOCOCCUS JANNASCHII
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009435 | biological_process | NAD+ biosynthetic process |
| B | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009435 | biological_process | NAD+ biosynthetic process |
| C | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0009435 | biological_process | NAD+ biosynthetic process |
| D | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0009435 | biological_process | NAD+ biosynthetic process |
| E | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009058 | biological_process | biosynthetic process |
| E | 0009435 | biological_process | NAD+ biosynthetic process |
| F | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009058 | biological_process | biosynthetic process |
| F | 0009435 | biological_process | NAD+ biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 706 |
| Chain | Residue |
| A | ATP700 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG D 707 |
| Chain | Residue |
| D | ATP703 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG C 708 |
| Chain | Residue |
| C | ATP702 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 709 |
| Chain | Residue |
| B | ATP701 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 800 |
| Chain | Residue |
| F | ATP705 |
| F | HOH869 |
| F | HOH879 |
| F | HOH941 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG E 801 |
| Chain | Residue |
| E | ATP704 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP A 700 |
| Chain | Residue |
| A | ILE5 |
| A | GLY7 |
| A | ARG8 |
| A | PHE9 |
| A | HIS13 |
| A | HIS16 |
| A | PRO116 |
| A | GLU117 |
| A | MET118 |
| A | PHE119 |
| A | ARG121 |
| A | TYR124 |
| A | SER125 |
| A | GLY126 |
| A | THR127 |
| A | ARG130 |
| A | MG706 |
| A | HOH736 |
| A | HOH741 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP B 701 |
| Chain | Residue |
| B | ILE5 |
| B | GLY7 |
| B | ARG8 |
| B | PHE9 |
| B | HIS13 |
| B | HIS16 |
| B | PRO116 |
| B | GLU117 |
| B | MET118 |
| B | PHE119 |
| B | ARG121 |
| B | TYR124 |
| B | SER125 |
| B | GLY126 |
| B | THR127 |
| B | ARG130 |
| B | MG709 |
| B | HOH744 |
| B | HOH765 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP C 702 |
| Chain | Residue |
| C | ILE5 |
| C | ILE6 |
| C | GLY7 |
| C | ARG8 |
| C | PHE9 |
| C | HIS13 |
| C | GLY15 |
| C | HIS16 |
| C | GLU117 |
| C | PHE119 |
| C | ARG121 |
| C | TYR124 |
| C | SER125 |
| C | GLY126 |
| C | THR127 |
| C | ARG130 |
| C | MG708 |
| C | HOH739 |
| C | HOH769 |
| site_id | BC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP D 703 |
| Chain | Residue |
| D | ILE5 |
| D | GLY7 |
| D | ARG8 |
| D | PHE9 |
| D | HIS13 |
| D | HIS16 |
| D | PRO116 |
| D | GLU117 |
| D | MET118 |
| D | PHE119 |
| D | ARG121 |
| D | TYR124 |
| D | SER125 |
| D | GLY126 |
| D | THR127 |
| D | ARG130 |
| D | MG707 |
| D | HOH745 |
| D | HOH768 |
| D | HOH786 |
| D | HOH798 |
| site_id | BC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP E 704 |
| Chain | Residue |
| E | PHE119 |
| E | ARG121 |
| E | TYR124 |
| E | SER125 |
| E | GLY126 |
| E | THR127 |
| E | ARG130 |
| E | MG801 |
| E | HOH860 |
| E | HOH917 |
| E | ILE5 |
| E | ILE6 |
| E | GLY7 |
| E | ARG8 |
| E | PHE9 |
| E | HIS13 |
| E | GLY15 |
| E | HIS16 |
| E | VAL19 |
| E | PRO116 |
| E | GLU117 |
| E | MET118 |
| site_id | BC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ATP F 705 |
| Chain | Residue |
| F | ILE5 |
| F | ILE6 |
| F | GLY7 |
| F | ARG8 |
| F | PHE9 |
| F | HIS13 |
| F | GLY15 |
| F | HIS16 |
| F | VAL19 |
| F | PRO116 |
| F | GLU117 |
| F | MET118 |
| F | PHE119 |
| F | ARG121 |
| F | TYR124 |
| F | SER125 |
| F | GLY126 |
| F | THR127 |
| F | ARG130 |
| F | MG800 |
| F | HOH811 |
| F | HOH829 |
| F | HOH941 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10986466","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F9A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
