Entry: Q9CCE3 Genes: ML0918 Length: 249 aa

Purine nucleoside phosphorylase ML0918

PURNU_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: Q9CCE3 ML Locus: ML0918
Entry Q9CCE3
Reviewed reviewed
Entry Name PURNU_MYCLE
Gene Names ML0918
ML locus tag ML0918
Organism Mycobacterium leprae (strain TN)
Length 249 aa
Mass 26305 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17574744;
KEGG mle:ML0918;
eggNOG COG1496;
OrthoDB 4279at2;
InterPro IPR003730;IPR038371;IPR011324;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML0918, 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 1XAF 0.736237 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 ML0918, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.766438 Download Model
Monomer AlphaFold‑3 1 0.855283 Download Model
Monomer Boltz 0 0.766495 Download Model
Monomer CHAI 1 0.184434 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* — ML0918

Mol* Structure Viewer

Local mmCIF model display for ML0918 with Mol* controls hidden.
Default: Homo 2-mer • Boltz2
Preparing Homo 2-mer • Boltz2 model 0 for ML0918…
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 2.4.2.1; 2.4.2.28; 3.5.4.4
Catalytic activity CATALYTIC ACTIVITY: Reaction=adenosine + phosphate = alpha-D-ribose 1-phosphate + adenine; Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000250|UniProtKB:P84138}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27643; Evidence={ECO:0000250|UniProtKB:P84138}; CATALYTIC ACTIVITY: Reaction=S-methyl-5'-thioadenosine + phosphate = 5-(methylsulfanyl)-alpha-D-ribose 1-phosphate + adenine; Xref=Rhea:RHEA:11852, ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474, ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000250|UniProtKB:P84138}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853; Evidence={ECO:0000250|UniProtKB:P84138}; CATALYTIC ACTIVITY: Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000250|UniProtKB:P84138}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647; Evidence={ECO:0000250|UniProtKB:P84138}; CATALYTIC ACTIVITY: Reaction=adenosine + H2O + H(+) = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000250|UniProtKB:P84138}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; Evidence={ECO:0000250|UniProtKB:P84138};
Binding site BINDING 72; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P84138"; BINDING 109; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P84138"; BINDING 126; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P84138"
Cofactor COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:P33644}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P84138};
Subunit structure SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q1EIR0}.
Annotation Summary

Ontology and localisation

Gene Ontology (GO) adenosine deaminase activity [GO:0004000]; copper ion binding [GO:0005507]; oxidoreductase activity [GO:0016491]; S-methyl-5-thioadenosine phosphorylase activity [GO:0017061]
Gene Ontology (molecular function) adenosine deaminase activity [GO:0004000]; copper ion binding [GO:0005507]; oxidoreductase activity [GO:0016491]; S-methyl-5-thioadenosine phosphorylase activity [GO:0017061]
Gene Ontology IDs GO:0004000; GO:0005507; GO:0016491; GO:0017061
Protein families Purine nucleoside phosphorylase YfiH/LACC1 family
Sequence similarities SIMILARITY: Belongs to the purine nucleoside phosphorylase YfiH/LACC1 family. {ECO:0000305}.
Annotation Summary

Sequence features and PTMs

Chain CHAIN 1..249; /note="Purine nucleoside phosphorylase ML0918"; /id="PRO_0000163165"