Entry: Q9CBQ3 Genes: adhA ML1730 Length: 362 aa

NADP-dependent alcohol dehydrogenase C

Q9CBQ3_MYCLE Mycobacterium leprae (strain TN)
Navigate Overview Model Scores RCSB 1D Mol* Pockets B-Cell Epitopes Function and interactions Ontology and localisation Sequence features and PTMs Evidence and cross-references

Summary

Download FASTA UniProt: Q9CBQ3 ML Locus: ML1730
Entry Q9CBQ3
Reviewed unreviewed
Entry Name Q9CBQ3_MYCLE
Gene Names adhA ML1730
ML locus tag ML1730
Organism Mycobacterium leprae (strain TN)
Length 362 aa
Mass 38908 Da
Annotation 2.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17575575;
KEGG mle:ML1730;
eggNOG COG1064;
OrthoDB 3567264at2;
InterPro IPR013149;IPR013154;IPR002328;IPR047109;IPR020843;IPR011032;IPR036291;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML1730, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 1
Assembly Method Template / Source Overall Rank Download
Homo 2-mer Boltz2 1UUF 0.931326 Download Model

Ligands

Curated ligands imported from the selected oligomer template/YAML rows. The displayed ligand code is the original template CCD code; predicted-model placeholders such as LIG1/LIG2 are not shown. Click a ligand code to focus the ligand in Mol*.
Ligands: 0
Ligand Code Ligand Name PubChem ID
No curated ligand rows were found for this oligomer in the database.

Monomer Models

Monomer structure models for ML1730, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.926531 Download Model
Monomer AlphaFold‑3 4 0.959289 Download Model
Monomer Boltz 0 0.928909 Download Model
Monomer CHAI 2 0.189505 Download Model

Sequence & Feature Viewer

Residue-level feature tracks for the loaded model — pLDDT confidence colouring, mapped annotations, and interactive PAE selection ranges. Drag a region on the heatmap to highlight it here and in Mol*.
RCSB 1D
Sequence viewer will initialise once a structure model is loaded.
Mol* — ML1730

Mol* Structure Viewer

Local mmCIF model display for ML1730 with Mol* controls hidden.
Default: Homo 2-mer • Boltz2
Preparing Homo 2-mer • Boltz2 model 0 for ML1730…
Residue focus: none
Heterooligomer ML IDs / chain selection

PAE Map Panel

Predicted aligned error heatmap for the currently loaded model, when pairwise confidence data are available in the local mmCIF.
PAE • Waiting for Model
PAE Heatmap
Loading pairwise confidence data for the selected model…
Scored residue
Aligned residue
Hover over the heatmap to inspect residue-pair PAE values.
Click a cell or drag across the heatmap to select residue blocks and mirror them in the sequence viewer.

B-cell Epitope Propensity

Per-residue conformational B-cell epitope predictions from DiscoTope-3.0.
Epitope · Loading
Low
Epitope
Residue number Residue type DiscoTope-3.0 score Focus
Loading epitope predictions…
Click a residue to focus it in Mol*.
Annotation Summary

Function and interactions

EC number 1.1.1.2
Catalytic activity CATALYTIC ACTIVITY: Reaction=a primary alcohol + NADP(+) = an aldehyde + NADPH + H(+); Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2; Evidence={ECO:0000256|ARBA:ARBA00048262};
Cofactor COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947, ECO:0000256|RuleBase:RU361277};
Annotation Summary

Ontology and localisation

Gene Ontology (GO) alcohol dehydrogenase (NADP+) activity [GO:0008106]; zinc ion binding [GO:0008270]
Gene Ontology (molecular function) alcohol dehydrogenase (NADP+) activity [GO:0008106]; zinc ion binding [GO:0008270]
Gene Ontology IDs GO:0008106; GO:0008270
Protein families Zinc-containing alcohol dehydrogenase family
Sequence similarities SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. {ECO:0000256|RuleBase:RU361277}.
Annotation Summary

Sequence features and PTMs

Domain [FT] DOMAIN 27..357; /note="Enoyl reductase (ER)"; /evidence="ECO:0000259|SMART:SM00829"