Entry: P46723 Genes: hemB ML2419 B2168_C3_264 Length: 329 aa

Delta-aminolevulinic acid dehydratase (ALAD) (ALADH)

HEM2_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: P46723 ML Locus: ML2419
Entry P46723
Reviewed reviewed
Entry Name HEM2_MYCLE
Gene Names hemB ML2419 B2168_C3_264
ML locus tag ML2419
Organism Mycobacterium leprae (strain TN)
Length 329 aa
Mass 34775 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17576281;
KEGG mle:ML2419;
eggNOG COG0113;
OrthoDB 9805001at2;
InterPro IPR001731;IPR030656;IPR013785;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML2419, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 1
Assembly Method Template / Source Overall Rank Download
Homo 8-mer Boltz2 5LZL 0.746474 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 ML2419, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.932434 Download Model
Monomer AlphaFold‑3 1 0.974025 Download Model
Monomer Boltz 0 0.925786 Download Model
Monomer CHAI 0 0.193574 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* — ML2419

Mol* Structure Viewer

Local mmCIF model display for ML2419 with Mol* controls hidden.
Default: Homo 8-mer • Boltz2
Preparing Homo 8-mer • Boltz2 model 0 for ML2419…
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 4.2.1.24
Pathway PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Catalytic activity CATALYTIC ACTIVITY: Reaction=2 5-aminolevulinate = porphobilinogen + 2 H2O + H(+); Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24;
Binding site BINDING 212; /ligand="5-aminolevulinate"; /ligand_id="ChEBI:CHEBI:356416"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 223; /ligand="5-aminolevulinate"; /ligand_id="ChEBI:CHEBI:356416"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 239; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 280; /ligand="5-aminolevulinate"; /ligand_id="ChEBI:CHEBI:356416"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 319; /ligand="5-aminolevulinate"; /ligand_id="ChEBI:CHEBI:356416"; /ligand_label="2"; /evidence="ECO:0000250"
Active site ACT_SITE 202; /note="Schiff-base intermediate with substrate"; /evidence="ECO:0000250"; ACT_SITE 254; /note="Schiff-base intermediate with substrate"; /evidence="ECO:0000250"
Subunit structure SUBUNIT: Homooctamer. {ECO:0000250}.
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) protoporphyrinogen IX biosynthetic process [GO:0006782]
Gene Ontology (cellular component) cytosol [GO:0005829]
Gene Ontology (GO) cytosol [GO:0005829]; porphobilinogen synthase activity [GO:0004655]; zinc ion binding [GO:0008270]; protoporphyrinogen IX biosynthetic process [GO:0006782]
Gene Ontology (molecular function) porphobilinogen synthase activity [GO:0004655]; zinc ion binding [GO:0008270]
Gene Ontology IDs GO:0004655; GO:0005829; GO:0006782; GO:0008270
Protein families ALAD family
Sequence similarities SIMILARITY: Belongs to the ALAD family. {ECO:0000305}.
Annotation Summary

Sequence features and PTMs

Chain CHAIN 1..329; /note="Delta-aminolevulinic acid dehydratase"; /id="PRO_0000140504"