7BU2
Structure of alcohol dehydrogenase YjgB from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006629 | biological_process | lipid metabolic process |
| 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 | 0006629 | biological_process | lipid metabolic process |
| 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 | 8 |
| Details | binding site for residue NO3 A 401 |
| Chain | Residue |
| A | SER74 |
| A | ALA75 |
| A | ALA76 |
| A | GLN77 |
| A | ASP78 |
| A | LYS79 |
| A | HOH730 |
| B | GLU25 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | CYS152 |
| A | ALA286 |
| A | HOH532 |
| A | HOH599 |
| A | HOH694 |
| A | SER43 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | THR169 |
| A | ARG171 |
| A | GLU194 |
| B | LYS295 |
| B | ARG298 |
| B | PHE299 |
| B | ARG302 |
| B | HOH513 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | GLY105 |
| A | THR289 |
| A | TYR291 |
| A | GLU292 |
| A | HOH534 |
| A | HOH535 |
| A | HOH682 |
| B | SER104 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | ILE108 |
| A | LYS159 |
| A | ILE276 |
| A | ALA277 |
| A | ASP279 |
| A | SER285 |
| A | ALA286 |
| A | THR287 |
| A | HOH566 |
| A | HOH583 |
| A | HOH668 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 406 |
| Chain | Residue |
| A | CYS41 |
| A | HIS63 |
| A | GLU64 |
| A | CYS152 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 407 |
| Chain | Residue |
| A | CYS96 |
| A | CYS99 |
| A | CYS102 |
| A | CYS110 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue NO3 B 401 |
| Chain | Residue |
| B | SER315 |
| B | LYS316 |
| B | ILE317 |
| B | ASN318 |
| B | ASP319 |
| B | HOH632 |
| B | HOH672 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | ILE108 |
| B | ASN109 |
| B | LYS159 |
| B | ILE276 |
| B | ALA277 |
| B | ASP279 |
| B | SER285 |
| B | ALA286 |
| B | THR287 |
| B | HOH585 |
| B | HOH595 |
| B | HOH617 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | SER43 |
| B | TRP91 |
| B | CYS152 |
| B | ALA286 |
| B | HOH502 |
| B | HOH520 |
| B | HOH530 |
| B | HOH667 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 404 |
| Chain | Residue |
| B | CYS96 |
| B | CYS99 |
| B | CYS102 |
| B | CYS110 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 405 |
| Chain | Residue |
| B | CYS41 |
| B | HIS63 |
| B | GLU64 |
| B | CYS152 |
| B | HOH502 |
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 |
| 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
