Entry: Q9CC57 Genes: hisD ML1257 MLCB1610.20 Length: 449 aa

Histidinol dehydrogenase (HDH)

HISX_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: Q9CC57 ML Locus: ML1257
Entry Q9CC57
Reviewed reviewed
Entry Name HISX_MYCLE
Gene Names hisD ML1257 MLCB1610.20
ML locus tag ML1257
Organism Mycobacterium leprae (strain TN)
Length 449 aa
Mass 46828 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17575089;
KEGG mle:ML1257;
eggNOG COG0141;
OrthoDB 9805269at2;
InterPro IPR016161;IPR001692;IPR022695;IPR012131;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML1257, 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 4G09 0.941518 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 ML1257, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.943178 Download Model
Monomer AlphaFold‑3 1 0.942746 Download Model
Monomer Boltz 0 0.941548 Download Model
Monomer CHAI 2 0.190124 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* — ML1257

Mol* Structure Viewer

Local mmCIF model display for ML1257 with Mol* controls hidden.
Default: Homo 2-mer • Boltz2
Preparing Homo 2-mer • Boltz2 model 0 for ML1257…
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
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Scored residue
Aligned residue
Hover over the heatmap to inspect residue-pair PAE values.
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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
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Annotation Summary

Function and interactions

EC number 1.1.1.23
Pathway PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
Catalytic activity CATALYTIC ACTIVITY: Reaction=L-histidinol + 2 NAD(+) + H2O = L-histidine + 2 NADH + 3 H(+); Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23;
Binding site BINDING 136; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 204; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 232; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 255; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 277; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 277; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 280; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 280; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 347; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 380; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 380; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 434; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 439; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 439; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"
Cofactor COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
Active site ACT_SITE 346; /note="Proton acceptor"; /evidence="ECO:0000250"; ACT_SITE 347; /note="Proton acceptor"; /evidence="ECO:0000250"
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) L-histidine biosynthetic process [GO:0000105]
Gene Ontology (cellular component) cytosol [GO:0005829]
Gene Ontology (GO) cytosol [GO:0005829]; histidinol dehydrogenase activity [GO:0004399]; NAD binding [GO:0051287]; zinc ion binding [GO:0008270]; L-histidine biosynthetic process [GO:0000105]
Gene Ontology (molecular function) histidinol dehydrogenase activity [GO:0004399]; NAD binding [GO:0051287]; zinc ion binding [GO:0008270]
Gene Ontology IDs GO:0000105; GO:0004399; GO:0005829; GO:0008270; GO:0051287
Protein families Histidinol dehydrogenase family
Sequence similarities SIMILARITY: Belongs to the histidinol dehydrogenase family. {ECO:0000305}.
Annotation Summary

Sequence features and PTMs

Chain CHAIN 1..449; /note="Histidinol dehydrogenase"; /id="PRO_0000135796"