1BW9
PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND PHENYLPYRUVATE
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 | 5 |
Details | BINDING SITE FOR RESIDUE K B 850 |
Chain | Residue |
A | ASP118 |
A | THR121 |
A | HOH656 |
A | HOH728 |
B | HOH884 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 851 |
Chain | Residue |
B | HOH1227 |
B | HOH1319 |
A | HOH371 |
A | HOH436 |
B | ASP409 |
B | HOH1100 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 852 |
Chain | Residue |
B | GLN600 |
B | GLY618 |
B | HOH1008 |
B | HOH1083 |
B | HOH1326 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K B 853 |
Chain | Residue |
B | LEU570 |
B | SER572 |
B | ASP574 |
B | LEU576 |
B | PO4880 |
B | HOH993 |
B | HOH1140 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PO4 B 880 |
Chain | Residue |
B | SER401 |
B | SER404 |
B | LYS458 |
B | LEU570 |
B | LEU576 |
B | K853 |
B | HOH1019 |
B | HOH1038 |
B | HOH1140 |
B | HOH1157 |
B | HOH1204 |
site_id | AC6 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAD A 360 |
Chain | Residue |
A | LYS66 |
A | LYS78 |
A | PRO117 |
A | ASP118 |
A | VAL119 |
A | GLY182 |
A | GLY184 |
A | ALA185 |
A | VAL186 |
A | ALA204 |
A | ASP205 |
A | THR206 |
A | ARG210 |
A | LEU224 |
A | CYS238 |
A | ALA239 |
A | MET240 |
A | ALA260 |
A | ALA261 |
A | ASN262 |
A | PPY361 |
A | HOH394 |
A | HOH395 |
A | HOH446 |
A | HOH493 |
A | HOH521 |
A | HOH552 |
A | HOH656 |
A | HOH761 |
A | HOH771 |
B | EDO874 |
B | HOH881 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PPY A 361 |
Chain | Residue |
A | GLY39 |
A | GLY40 |
A | MET63 |
A | LYS66 |
A | LYS78 |
A | GLY116 |
A | PRO117 |
A | GLY291 |
A | ALA292 |
A | LEU295 |
A | NAD360 |
A | HOH414 |
B | HOH882 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NAD B 760 |
Chain | Residue |
B | LEU583 |
B | GLY584 |
B | ALA585 |
B | VAL586 |
B | ASP605 |
B | THR606 |
B | ARG610 |
B | HOH905 |
B | HOH907 |
B | HOH935 |
B | HOH1044 |
B | HOH1239 |
B | HOH1381 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PPY B 761 |
Chain | Residue |
B | PRO517 |
A | HOH382 |
B | GLY439 |
B | GLY440 |
B | MET463 |
B | LYS466 |
B | LYS478 |
B | GLY516 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 871 |
Chain | Residue |
B | MET474 |
B | IPA861 |
B | HOH1193 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 873 |
Chain | Residue |
A | HOH600 |
B | HOH887 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 874 |
Chain | Residue |
A | SER149 |
A | ALA150 |
A | THR153 |
A | VAL186 |
A | NAD360 |
B | HOH881 |
B | HOH882 |
B | HOH884 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPA B 860 |
Chain | Residue |
A | CYS232 |
A | ASP253 |
A | CYS254 |
A | SER255 |
A | HOH610 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPA B 861 |
Chain | Residue |
A | ALA276 |
B | LEU434 |
B | PRO473 |
B | EDO871 |
B | HOH1071 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPA B 862 |
Chain | Residue |
B | ARG442 |
B | ASP455 |
B | LYS458 |
B | LEU459 |
B | ASN663 |
B | HOH1123 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPA B 863 |
Chain | Residue |
A | THR15 |
A | LEU49 |
B | LEU406 |
B | ARG428 |
B | HOH985 |
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 |