1XNH
Crystal Structure of NH3-dependent NAD+ synthetase from Helicobacter pylori
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008795 | molecular_function | NAD+ synthase activity |
| A | 0009435 | biological_process | NAD+ biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00193","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15645437","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00193","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
