1BXG
PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND BETA-PHENYLPROPIONATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006559 | biological_process | L-phenylalanine catabolic process |
| A | 0009094 | biological_process | L-phenylalanine 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 | 0050175 | molecular_function | phenylalanine dehydrogenase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006559 | biological_process | L-phenylalanine catabolic process |
| B | 0009094 | biological_process | L-phenylalanine 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 | 0050175 | molecular_function | phenylalanine dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K B 850 |
| Chain | Residue |
| B | HOH111 |
| B | HOH151 |
| B | LEU570 |
| B | SER572 |
| B | ASP574 |
| B | LEU576 |
| B | PO4900 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 900 |
| Chain | Residue |
| B | LYS458 |
| B | LEU570 |
| B | K850 |
| B | SER401 |
| B | SER404 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD A 360 |
| Chain | Residue |
| A | SER149 |
| A | THR153 |
| A | GLY182 |
| A | GLY184 |
| A | ALA185 |
| A | VAL186 |
| A | ASP205 |
| A | THR206 |
| A | CYS238 |
| A | ALA239 |
| A | MET240 |
| A | ALA260 |
| A | ALA261 |
| A | ASN288 |
| A | HCI361 |
| A | HOH401 |
| A | HOH426 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE HCI A 361 |
| Chain | Residue |
| A | GLY39 |
| A | GLY40 |
| A | LYS66 |
| A | LYS78 |
| A | GLY116 |
| A | ASN262 |
| A | NAD360 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD B 760 |
| Chain | Residue |
| B | HOH4 |
| B | HOH36 |
| B | ARG442 |
| B | SER549 |
| B | THR553 |
| B | GLY582 |
| B | LEU583 |
| B | GLY584 |
| B | ALA585 |
| B | VAL586 |
| B | ALA604 |
| B | ASP605 |
| B | THR606 |
| B | ARG610 |
| B | LEU624 |
| B | CYS638 |
| B | ALA639 |
| B | ALA660 |
| B | ALA661 |
| B | ASN662 |
| B | ASN688 |
| B | HCI761 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HCI B 761 |
| Chain | Residue |
| B | HOH27 |
| B | HOH36 |
| B | GLY439 |
| B | GLY440 |
| B | LYS466 |
| B | LYS478 |
| B | GLY516 |
| B | ASN662 |
| B | NAD760 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10924111 |
| Chain | Residue | Details |
| B | LYS478 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10924111, ECO:0007744|PDB:1C1D |
| Chain | Residue | Details |
| B | ASN662 | |
| B | ARG442 | |
| B | LYS466 | |
| B | PRO517 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10924111, ECO:0007744|PDB:1BXG, ECO:0007744|PDB:1C1D, ECO:0007744|PDB:1C1X |
| Chain | Residue | Details |
| B | SER549 | |
| B | THR553 | |
| B | ASP518 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10924111, ECO:0000305, ECO:0007744|PDB:1BW9, ECO:0007744|PDB:1BXG, ECO:0007744|PDB:1C1D |
| Chain | Residue | Details |
| B | GLY582 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10924111, ECO:0007744|PDB:1BW9, ECO:0007744|PDB:1BXG, ECO:0007744|PDB:1C1D |
| Chain | Residue | Details |
| B | ALA639 | |
| B | ALA660 | |
| B | ASP605 | |
| B | ARG610 |
