1J5P
Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009435 | biological_process | NAD+ biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0033735 | molecular_function | aspartate dehydrogenase [NAD(P)+] activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD A 300 |
| Chain | Residue |
| A | GLY7 |
| A | SER57 |
| A | PRO58 |
| A | ALA60 |
| A | GLU63 |
| A | TYR64 |
| A | ILE78 |
| A | SER79 |
| A | ALA109 |
| A | ASN164 |
| A | VAL165 |
| A | GLY9 |
| A | THR223 |
| A | HOH313 |
| A | HOH314 |
| A | HOH367 |
| A | HOH375 |
| A | ASN10 |
| A | ILE11 |
| A | ASP28 |
| A | ARG29 |
| A | ILE30 |
| A | CYS55 |
| A | ALA56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01265","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12496312","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12496312","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2002","submissionDatabase":"PDB data bank","title":"Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}},{"source":"PDB","id":"1H2H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1J5P","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01265","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12496312","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2002","submissionDatabase":"PDB data bank","title":"Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}},{"source":"PDB","id":"1H2H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1J5P","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
