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 | L-phenylalanine dehydrogenase (NAD+) activity |
| A | 0170033 | biological_process | L-amino acid metabolic process |
| A | 0170039 | biological_process | proteinogenic amino acid metabolic process |
| 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 | L-phenylalanine dehydrogenase (NAD+) activity |
| B | 0170033 | biological_process | L-amino acid metabolic process |
| B | 0170039 | biological_process | proteinogenic amino acid metabolic process |
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 | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"10924111","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10924111","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1C1D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10924111","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BXG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1C1D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1C1X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10924111","evidenceCode":"ECO:0000269"},{"evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1BW9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BXG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1C1D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10924111","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BW9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BXG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1C1D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hrd |
| Chain | Residue | Details |
| A | ASP118 | |
| A | LYS78 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hrd |
| Chain | Residue | Details |
| B | ASP518 | |
| B | LYS478 |
