2DC1
Crystal Structure Of L-Aspartate Dehydrogenase From Hyperthermophilic Archaeon Archaeoglobus fulgidus
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 | L-aspartate dehydrogenase [NAD(P)+] activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0009435 | biological_process | NAD+ biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| B | 0033735 | molecular_function | L-aspartate dehydrogenase [NAD(P)+] activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CIT A 1585 |
| Chain | Residue |
| A | ALA111 |
| A | NAD242 |
| A | HOH1623 |
| A | HOH1627 |
| A | ASN160 |
| A | LEU161 |
| A | ASN162 |
| A | VAL163 |
| A | HIS189 |
| A | LYS214 |
| A | THR215 |
| A | SER216 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CIT B 2585 |
| Chain | Residue |
| B | ALA1111 |
| B | LYS1134 |
| B | ASN1160 |
| B | LEU1161 |
| B | ASN1162 |
| B | VAL1163 |
| B | ASN1187 |
| B | HIS1189 |
| B | LYS1214 |
| B | SER1216 |
| B | NAD1242 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD A 242 |
| Chain | Residue |
| A | GLY7 |
| A | GLY9 |
| A | ALA10 |
| A | ILE11 |
| A | ASP31 |
| A | VAL32 |
| A | ALA58 |
| A | SER59 |
| A | ALA62 |
| A | TYR66 |
| A | LEU80 |
| A | SER81 |
| A | GLY110 |
| A | ALA111 |
| A | ASN162 |
| A | ASN212 |
| A | THR215 |
| A | ALA219 |
| A | CIT1585 |
| A | HOH1590 |
| A | HOH1597 |
| A | HOH1599 |
| A | HOH1644 |
| A | HOH1652 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD B 1242 |
| Chain | Residue |
| B | HOH5 |
| B | HOH26 |
| B | HOH38 |
| B | HOH119 |
| B | HOH125 |
| B | GLY1007 |
| B | GLY1009 |
| B | ALA1010 |
| B | ILE1011 |
| B | ARG1021 |
| B | ASP1031 |
| B | VAL1032 |
| B | ARG1033 |
| B | ALA1058 |
| B | SER1059 |
| B | ALA1062 |
| B | TYR1066 |
| B | LEU1080 |
| B | SER1081 |
| B | GLY1110 |
| B | ALA1111 |
| B | ASN1162 |
| B | VAL1163 |
| B | ASN1212 |
| B | THR1215 |
| B | ALA1219 |
| B | CIT2585 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01265","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17651440","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DC1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01265","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17651440","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DC1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2DC1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
