4WE3
STRUCTURE OF THE BINARY COMPLEX OF A ZINGIBER OFFICINALE DOUBLE BOND REDUCTASE IN COMPLEX WITH NADP MONOCLINIC CRYSTAL FORM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006950 | biological_process | response to stress |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| A | 0032440 | molecular_function | 2-alkenal reductase [NAD(P)H] activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006950 | biological_process | response to stress |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| B | 0032440 | molecular_function | 2-alkenal reductase [NAD(P)H] activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0006950 | biological_process | response to stress |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| C | 0032440 | molecular_function | 2-alkenal reductase [NAD(P)H] activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0006950 | biological_process | response to stress |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| D | 0032440 | molecular_function | 2-alkenal reductase [NAD(P)H] activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue NAP A 400 |
| Chain | Residue |
| A | PRO60 |
| A | LYS197 |
| A | TYR213 |
| A | ASN237 |
| A | VAL238 |
| A | CYS259 |
| A | GLY260 |
| A | PHE289 |
| A | LEU290 |
| A | VAL291 |
| A | ASN339 |
| A | MET143 |
| A | HOH513 |
| A | HOH522 |
| A | HOH530 |
| A | HOH531 |
| A | HOH533 |
| A | THR147 |
| A | ALA168 |
| A | GLY171 |
| A | ALA172 |
| A | VAL173 |
| A | ALA192 |
| A | GLY193 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | binding site for residue NAP B 400 |
| Chain | Residue |
| B | PRO60 |
| B | THR147 |
| B | GLY171 |
| B | ALA172 |
| B | VAL173 |
| B | ALA192 |
| B | GLY193 |
| B | LYS197 |
| B | TYR213 |
| B | ASN237 |
| B | CYS259 |
| B | GLY260 |
| B | ILE262 |
| B | SER263 |
| B | TYR265 |
| B | PHE289 |
| B | VAL291 |
| B | PHE335 |
| B | ASN339 |
| B | HOH510 |
| B | HOH519 |
| B | HOH527 |
| B | HOH528 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | binding site for residue NAP C 400 |
| Chain | Residue |
| C | PRO60 |
| C | MET143 |
| C | THR147 |
| C | GLY171 |
| C | ALA172 |
| C | VAL173 |
| C | ALA192 |
| C | GLY193 |
| C | LYS197 |
| C | TYR213 |
| C | ASN237 |
| C | VAL238 |
| C | CYS259 |
| C | GLY260 |
| C | MET261 |
| C | ILE262 |
| C | SER263 |
| C | TYR265 |
| C | PHE289 |
| C | LEU290 |
| C | VAL291 |
| C | LEU334 |
| C | PHE335 |
| C | GLY337 |
| C | ASN339 |
| C | HOH507 |
| C | HOH510 |
| C | HOH511 |
| C | HOH534 |
| C | HOH540 |
| C | HOH551 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | binding site for residue NAP D 400 |
| Chain | Residue |
| D | HOH505 |
| D | HOH508 |
| D | HOH512 |
| D | HOH523 |
| D | HOH528 |
| D | PRO60 |
| D | MET143 |
| D | THR147 |
| D | GLY171 |
| D | ALA172 |
| D | VAL173 |
| D | ALA192 |
| D | GLY193 |
| D | LYS197 |
| D | TYR213 |
| D | ASN237 |
| D | CYS259 |
| D | GLY260 |
| D | ILE262 |
| D | TYR265 |
| D | PHE289 |
| D | VAL291 |
| D | LEU334 |
| D | PHE335 |
| D | ASN339 |
| D | HOH503 |
