7BU3
Structure of alcohol dehydrogenase YjgB in complex with NADP from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue ASP A 401 |
| Chain | Residue |
| A | MET314 |
| A | SER315 |
| A | LYS336 |
| A | ALA337 |
| A | HOH502 |
| A | HOH506 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | binding site for residue NAP A 402 |
| Chain | Residue |
| A | CYS152 |
| A | THR156 |
| A | GLY176 |
| A | ILE177 |
| A | GLY178 |
| A | GLY179 |
| A | LEU180 |
| A | SER199 |
| A | SER200 |
| A | ASN201 |
| A | LYS204 |
| A | THR238 |
| A | VAL239 |
| A | ASN240 |
| A | VAL241 |
| A | VAL261 |
| A | ALA263 |
| A | SER285 |
| A | ALA286 |
| A | THR287 |
| A | ARG332 |
| A | PEG404 |
| A | HOH534 |
| A | HOH556 |
| A | HOH589 |
| A | HOH609 |
| A | HOH637 |
| A | HOH642 |
| A | HOH672 |
| B | ARG220 |
| A | HIS42 |
| A | SER43 |
| A | TRP52 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | SER199 |
| A | SER200 |
| A | ASN201 |
| A | PRO202 |
| A | GLU205 |
| A | ASN218 |
| A | ARG220 |
| A | HOH688 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue PEG A 404 |
| Chain | Residue |
| A | TRP52 |
| A | TRP91 |
| A | PHE273 |
| A | NAP402 |
| A | HOH516 |
| A | HOH548 |
| A | HOH562 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 405 |
| Chain | Residue |
| A | CYS41 |
| A | HIS63 |
| A | GLU64 |
| A | CYS152 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 406 |
| Chain | Residue |
| A | CYS96 |
| A | CYS99 |
| A | CYS102 |
| A | CYS110 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | binding site for residue NAP B 401 |
| Chain | Residue |
| A | ARG220 |
| B | HIS42 |
| B | SER43 |
| B | TRP52 |
| B | CYS152 |
| B | THR156 |
| B | GLY176 |
| B | ILE177 |
| B | GLY178 |
| B | GLY179 |
| B | LEU180 |
| B | SER199 |
| B | SER200 |
| B | LYS204 |
| B | ARG220 |
| B | THR238 |
| B | VAL239 |
| B | ASN240 |
| B | VAL241 |
| B | VAL261 |
| B | GLY262 |
| B | ALA263 |
| B | SER285 |
| B | ALA286 |
| B | THR287 |
| B | ARG332 |
| B | PEG402 |
| B | HOH535 |
| B | HOH576 |
| B | HOH580 |
| B | HOH604 |
| B | HOH628 |
| B | HOH654 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue PEG B 402 |
| Chain | Residue |
| B | NAP401 |
| B | HOH556 |
| B | HOH603 |
| B | TRP52 |
| B | TRP91 |
| B | PHE273 |
| B | ILE276 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | SER199 |
| B | SER200 |
| B | ASN201 |
| B | PRO202 |
| B | GLU205 |
| B | VAL216 |
| B | ASN218 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 404 |
| Chain | Residue |
| B | CYS41 |
| B | HIS63 |
| B | GLU64 |
| B | CYS152 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 405 |
| Chain | Residue |
| B | CYS96 |
| B | GLY97 |
| B | CYS99 |
| B | CYS102 |
| B | CYS110 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEvIGRvvalGsaA |
| Chain | Residue | Details |
| A | GLY62-ALA76 | |
| B | GLY62-ALA76 |
| site_id | PS00065 |
| Number of Residues | 28 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGVIGiGGLGhiaikllhamgce.VTaFS |
| Chain | Residue | Details |
| A | VAL172-SER199 | |
| B | VAL172-SER199 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | CYS38 | |
| B | HIS63 | |
| B | CYS96 | |
| B | CYS99 | |
| B | CYS102 | |
| B | CYS110 | |
| B | CYS152 |
