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 | aspartate dehydrogenase 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 | aspartate dehydrogenase 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 | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01265 |
Chain | Residue | Details |
A | HIS189 | |
B | HIS1189 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17651440, ECO:0007744|PDB:2DC1 |
Chain | Residue | Details |
A | ALA10 | |
B | LEU1080 | |
A | ASP31 | |
A | ALA58 | |
A | TYR66 | |
A | LEU80 | |
B | ALA1010 | |
B | ASP1031 | |
B | ALA1058 | |
B | TYR1066 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000269|PubMed:17651440, ECO:0007744|PDB:2DC1 |
Chain | Residue | Details |
A | ALA111 | |
A | ASN162 | |
B | ALA1111 | |
B | ASN1162 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0007744|PDB:2DC1 |
Chain | Residue | Details |
A | ASN212 | |
B | ASN1212 |