4HFN
X-ray Crystal Structure of a Ternary Complex of Double Bond Reductase from Nicotiana tabacum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| A | 0035798 | molecular_function | 2-alkenal reductase (NADPH) activity |
| 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 |
| B | 0035798 | molecular_function | 2-alkenal reductase (NADPH) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NAP A 400 |
| Chain | Residue |
| A | PRO54 |
| A | TYR206 |
| A | GLN210 |
| A | ASN230 |
| A | CYS252 |
| A | GLY253 |
| A | MET254 |
| A | ILE255 |
| A | SER256 |
| A | TYR258 |
| A | PHE282 |
| A | MET136 |
| A | LEU283 |
| A | VAL284 |
| A | LEU327 |
| A | PHE328 |
| A | GLY330 |
| A | ASN332 |
| A | CIY401 |
| A | HOH501 |
| A | HOH502 |
| A | HOH503 |
| A | THR140 |
| A | HOH505 |
| A | HOH515 |
| A | HOH524 |
| A | HOH525 |
| A | HOH537 |
| A | HOH551 |
| A | HOH632 |
| A | HOH663 |
| A | GLY164 |
| A | ALA165 |
| A | VAL166 |
| A | ALA185 |
| A | GLY186 |
| A | LYS190 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CIY A 401 |
| Chain | Residue |
| A | TYR55 |
| A | TYR258 |
| A | LEU283 |
| A | PHE285 |
| A | NAP400 |
| A | HOH601 |
| A | HOH632 |
| B | PHE270 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP B 400 |
| Chain | Residue |
| B | PRO54 |
| B | MET136 |
| B | THR140 |
| B | GLY164 |
| B | ALA165 |
| B | VAL166 |
| B | ALA185 |
| B | GLY186 |
| B | LYS190 |
| B | TYR206 |
| B | ASN230 |
| B | CYS252 |
| B | GLY253 |
| B | ILE255 |
| B | PHE282 |
| B | LEU283 |
| B | VAL284 |
| B | GLY334 |
| B | HOH505 |
| B | HOH519 |
| B | HOH521 |
| B | HOH533 |
| B | HOH550 |
| B | HOH563 |
| B | HOH587 |
| B | HOH603 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2013","firstPage":"370","lastPage":"379","volume":"3","journal":"ACS Catal.","title":"Biocatalytic asymmetric alkene reduction: crystal structure and characterization of a double bond reductase from Nicotiana tabacum.","authors":["Mansell D.J.","Toogood H.S.","Waller J.","Hughes J.M.X.","Levy C.W.","Gardiner J.M.","Scrutton N.S."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/cs300709m"}]}}]} |
| Chain | Residue | Details |
