Entry: P30768 Genes: tuf ML1877 Length: 396 aa

Elongation factor Tu (EF-Tu)

EFTU_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: P30768 ML Locus: ML1877
Entry P30768
Reviewed reviewed
Entry Name EFTU_MYCLE
Gene Names tuf ML1877
ML locus tag ML1877
Organism Mycobacterium leprae (strain TN)
Length 396 aa
Mass 43668 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 8341612; 8446028; 8089081; 11234002
DOI ID 10.1093/nar/21.14.3327; 10.1111/j.1365-2958.1993.tb01112.x; 10.1093/oxfordjournals.jbchem.a124393; 10.1038/35059006
STRING 272631.gene:17575725;
KEGG mle:ML1877;
eggNOG COG0050;
OrthoDB 9803139at2;
InterPro IPR041709;IPR050055;IPR004161;IPR033720;IPR031157;IPR027417;IPR005225;IPR000795;IPR009000;IPR009001;IPR004541;IPR004160;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML1877, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 1
Assembly Method Template / Source Overall Rank Download
Hetero 2-mer Boltz2 7VMX 0.863098 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 ML1877, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.855192 Download Model
Monomer AlphaFold‑3 2 0.906757 Download Model
Monomer Boltz 0 0.859152 Download Model
Monomer CHAI 0 0.162781 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* — ML1877

Mol* Structure Viewer

Local mmCIF model display for ML1877 with Mol* controls hidden.
Default: Hetero 2-mer • Boltz2
Preparing Hetero 2-mer • Boltz2 model 0 for ML1877…
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 3.6.5.3
Catalytic activity CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00118}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000255|HAMAP-Rule:MF_00118};
Binding site BINDING 19..26; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_00118"; BINDING 26; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_00118"; BINDING 83..87; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_00118"; BINDING 138..141; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
Subunit structure SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
Annotation Summary

Ontology and localisation

Gene Ontology (cellular component) cytosol [GO:0005829]
Gene Ontology (GO) cytosol [GO:0005829]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; translation elongation factor activity [GO:0003746]
Gene Ontology (molecular function) GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; translation elongation factor activity [GO:0003746]
Gene Ontology IDs GO:0000287; GO:0003746; GO:0003924; GO:0005525; GO:0005829
Subcellular location [CC] SUBCELLULAR LOCATION: Cytoplasm.
Protein families TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily
Sequence similarities SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}.
Annotation Summary

Sequence features and PTMs

Chain CHAIN 1..396; /note="Elongation factor Tu"; /id="PRO_0000091348"
Region REGION 19..26; /note="G1"; /evidence="ECO:0000250"; REGION 62..66; /note="G2"; /evidence="ECO:0000250"; REGION 83..86; /note="G3"; /evidence="ECO:0000250"; REGION 138..141; /note="G4"; /evidence="ECO:0000250"; REGION 175..177; /note="G5"; /evidence="ECO:0000250"
Domain [FT] DOMAIN 10..205; /note="tr-type G"