Entry: O32956 Genes: pepA ML0864 MLCB22.14 Length: 524 aa

Probable cytosol aminopeptidase

AMPA_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: O32956 ML Locus: ML0864
Entry O32956
Reviewed reviewed
Entry Name AMPA_MYCLE
Gene Names pepA ML0864 MLCB22.14
ML locus tag ML0864
Organism Mycobacterium leprae (strain TN)
Length 524 aa
Mass 54342 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17574690;
KEGG mle:ML0864;
eggNOG COG0260;
OrthoDB 9809354at2;
InterPro IPR011356;IPR043472;IPR000819;IPR023042;IPR008283;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML0864, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 1
Assembly Method Template / Source Overall Rank Download
homo_6mer Boltz2 3H8G — 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 ML0864, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.945967 Download Model
Monomer AlphaFold‑3 2 0.958391 Download Model
Monomer Boltz 0 0.952202 Download Model
Monomer CHAI 0 0.192623 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* — ML0864

Mol* Structure Viewer

Local mmCIF model display for ML0864 with Mol* controls hidden.
Default: homo_6mer • Boltz2
Preparing homo_6mer • Boltz2 model 0 for ML0864…
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 3.4.11.1; 3.4.11.10
Catalytic activity CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10;
Binding site BINDING 288; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 293; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 293; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 311; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 370; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 372; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 372; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"
Cofactor COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250};
Active site ACT_SITE 300; /evidence="ECO:0000255"; ACT_SITE 374; /evidence="ECO:0000255"
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) proteolysis [GO:0006508]
Gene Ontology (cellular component) cytoplasm [GO:0005737]
Gene Ontology (GO) cytoplasm [GO:0005737]; manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; proteolysis [GO:0006508]
Gene Ontology (molecular function) manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]
Gene Ontology IDs GO:0005737; GO:0006508; GO:0030145; GO:0070006
Subcellular location [CC] SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Protein families Peptidase M17 family
Sequence similarities SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
Annotation Summary

Sequence features and PTMs

Chain CHAIN 1..524; /note="Probable cytosol aminopeptidase"; /id="PRO_0000165770"