6EOW
Structure of Raspberry Ketone Synthase with Hydroxybenzalacetone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006979 | biological_process | response to oxidative 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 | 0006979 | biological_process | response to oxidative 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 | 0006979 | biological_process | response to oxidative 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 | 0006979 | biological_process | response to oxidative 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 | 35 |
| Details | binding site for residue NAP A 401 |
| Chain | Residue |
| A | PRO58 |
| A | TYR211 |
| A | ASN235 |
| A | VAL236 |
| A | CYS257 |
| A | GLY258 |
| A | MET259 |
| A | ILE260 |
| A | SER261 |
| A | TYR263 |
| A | PHE287 |
| A | MET141 |
| A | MET288 |
| A | VAL289 |
| A | LEU332 |
| A | GLY335 |
| A | ASN337 |
| A | HOH525 |
| A | HOH544 |
| A | HOH548 |
| A | HOH551 |
| A | HOH571 |
| A | THR145 |
| A | HOH572 |
| A | HOH580 |
| A | HOH589 |
| A | HOH595 |
| A | HOH596 |
| A | HOH633 |
| A | GLY169 |
| A | ALA170 |
| A | VAL171 |
| A | ALA190 |
| A | GLY191 |
| A | LYS195 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue BKZ B 401 |
| Chain | Residue |
| B | TYR59 |
| B | MET141 |
| B | TYR263 |
| B | VAL289 |
| B | PHE290 |
| B | NAP402 |
| B | HOH614 |
| site_id | AC3 |
| Number of Residues | 37 |
| Details | binding site for residue NAP B 402 |
| Chain | Residue |
| B | PRO58 |
| B | MET141 |
| B | THR145 |
| B | GLY169 |
| B | ALA170 |
| B | VAL171 |
| B | ALA190 |
| B | GLY191 |
| B | LYS195 |
| B | TYR211 |
| B | ASN235 |
| B | VAL236 |
| B | CYS257 |
| B | GLY258 |
| B | MET259 |
| B | ILE260 |
| B | SER261 |
| B | TYR263 |
| B | PHE287 |
| B | MET288 |
| B | VAL289 |
| B | LEU332 |
| B | TYR333 |
| B | GLY335 |
| B | ASN337 |
| B | BKZ401 |
| B | HOH537 |
| B | HOH540 |
| B | HOH541 |
| B | HOH551 |
| B | HOH552 |
| B | HOH562 |
| B | HOH583 |
| B | HOH586 |
| B | HOH592 |
| B | HOH610 |
| B | HOH616 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue BKZ C 401 |
| Chain | Residue |
| C | TYR59 |
| C | TYR72 |
| C | MET141 |
| C | TYR263 |
| C | VAL289 |
| C | PHE290 |
| C | NAP402 |
| C | HOH501 |
| C | HOH596 |
| site_id | AC5 |
| Number of Residues | 35 |
| Details | binding site for residue NAP C 402 |
| Chain | Residue |
| C | VAL236 |
| C | CYS257 |
| C | GLY258 |
| C | ILE260 |
| C | SER261 |
| C | TYR263 |
| C | PHE287 |
| C | MET288 |
| C | VAL289 |
| C | LEU332 |
| C | GLY335 |
| C | ASN337 |
| C | BKZ401 |
| C | HOH529 |
| C | HOH531 |
| C | HOH532 |
| C | HOH534 |
| C | HOH546 |
| C | HOH548 |
| C | HOH580 |
| C | HOH581 |
| C | HOH583 |
| C | HOH585 |
| C | HOH613 |
| C | PRO58 |
| C | MET141 |
| C | THR145 |
| C | GLY169 |
| C | ALA170 |
| C | VAL171 |
| C | ALA190 |
| C | GLY191 |
| C | LYS195 |
| C | TYR211 |
| C | ASN235 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue BKZ D 401 |
| Chain | Residue |
| D | TYR59 |
| D | TYR85 |
| D | MET141 |
| D | TYR263 |
| D | VAL289 |
| D | PHE290 |
| D | NAP402 |
| D | HOH604 |
| site_id | AC7 |
| Number of Residues | 37 |
| Details | binding site for residue NAP D 402 |
| Chain | Residue |
| D | PRO58 |
| D | MET141 |
| D | THR145 |
| D | GLY169 |
| D | ALA170 |
| D | VAL171 |
| D | ALA190 |
| D | GLY191 |
| D | LYS195 |
| D | TYR211 |
| D | ASN235 |
| D | VAL236 |
| D | CYS257 |
| D | GLY258 |
| D | ILE260 |
| D | SER261 |
| D | TYR263 |
| D | PHE287 |
| D | MET288 |
| D | VAL289 |
| D | LEU332 |
| D | TYR333 |
| D | GLY335 |
| D | ASN337 |
| D | BKZ401 |
| D | HOH514 |
| D | HOH527 |
| D | HOH545 |
| D | HOH547 |
| D | HOH551 |
| D | HOH553 |
| D | HOH555 |
| D | HOH565 |
| D | HOH571 |
| D | HOH584 |
| D | HOH588 |
| D | HOH609 |
