Entry: Q9CBD3 Genes: cdd ML2174 Length: 134 aa

Cytidine deaminase

Q9CBD3_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: Q9CBD3 ML Locus: ML2174
Entry Q9CBD3
Reviewed unreviewed
Entry Name Q9CBD3_MYCLE
Gene Names cdd ML2174
ML locus tag ML2174
Organism Mycobacterium leprae (strain TN)
Length 134 aa
Mass 14251 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17576027;
KEGG mle:ML2174;
eggNOG COG0295;
OrthoDB 9795347at2;
InterPro IPR016192;IPR002125;IPR050202;IPR006262;IPR016193;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML2174, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 1
Assembly Method Template / Source Overall Rank Download
Homo 4-mer Boltz2 3R2N 0.730106 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 ML2174, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.920159 Download Model
Monomer AlphaFold‑3 0 0.928371 Download Model
Monomer Boltz 0 0.922235 Download Model
Monomer CHAI 3 0.183382 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* — ML2174

Mol* Structure Viewer

Local mmCIF model display for ML2174 with Mol* controls hidden.
Default: Homo 4-mer • Boltz2
Preparing Homo 4-mer • Boltz2 model 0 for ML2174…
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.
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 3.5.4.5
Catalytic activity CATALYTIC ACTIVITY: Reaction=2'-deoxycytidine + H2O + H(+) = 2'-deoxyuridine + NH4(+); Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5; Evidence={ECO:0000256|ARBA:ARBA00049252, ECO:0000256|RuleBase:RU364006}; CATALYTIC ACTIVITY: Reaction=cytidine + H2O + H(+) = uridine + NH4(+); Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5; Evidence={ECO:0000256|ARBA:ARBA00049558, ECO:0000256|RuleBase:RU364006};
Binding site BINDING 45..51; /ligand="substrate"; /evidence="ECO:0000256|PIRSR:PIRSR606262-2"; BINDING 56; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR606262-3"; BINDING 89; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR606262-3"; BINDING 92; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR606262-3"
Cofactor COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947, ECO:0000256|PIRSR:PIRSR606262-3, ECO:0000256|RuleBase:RU364006};
Active site ACT_SITE 58; /note="Proton donor"; /evidence="ECO:0000256|PIRSR:PIRSR606262-1"
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) nucleobase-containing small molecule metabolic process [GO:0055086]; pyrimidine-containing compound metabolic process [GO:0072527]
Gene Ontology (cellular component) cytosol [GO:0005829]
Gene Ontology (GO) cytosol [GO:0005829]; cytidine deaminase activity [GO:0004126]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270]; nucleobase-containing small molecule metabolic process [GO:0055086]; pyrimidine-containing compound metabolic process [GO:0072527]
Gene Ontology (molecular function) cytidine deaminase activity [GO:0004126]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270]
Gene Ontology IDs GO:0004126; GO:0005829; GO:0008270; GO:0042802; GO:0055086; GO:0072527
Protein families Cytidine and deoxycytidylate deaminase family
Sequence similarities SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family. {ECO:0000256|ARBA:ARBA00006576, ECO:0000256|RuleBase:RU364006}.
Annotation Summary

Sequence features and PTMs

Domain [FT] DOMAIN 4..126; /note="CMP/dCMP-type deaminase"; /evidence="ECO:0000259|PROSITE:PS51747"