Overview
Basic information about this protein and its source genome.
- Accession
- PA0353
- Gene
- PA0353 ilvD
- Status
- annotated
- Amino acids
- 612
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- Localization
- Cytoplasmic
Selected Druggability evidence
Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
9- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
- GO:0004160 Catalysis of the reaction: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O.
- GO:0016836 Catalysis of the cleavage of a carbon-oxygen bond by elimination of water.
- GO:0000287 Binding to a magnesium (Mg) ion.
- GO:0009097 OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
- GO:0009099 The chemical reactions and pathways resulting in the formation of valine, 2-amino-3-methylbutanoic acid.
- GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
- GO:0009082 The chemical reactions and pathways resulting in the formation of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 4 | 606 | Hamap | MF_00012 | Dihydroxy-acid dehydratase [ilvD]. |
| 4 | 606 | InterPro | IPR004404 | Dihydroxy-acid dehydratase |
| 18 | 606 | NCBIfam | TIGR00110 | dihydroxy-acid dehydratase |
| 18 | 606 | InterPro | IPR004404 | Dihydroxy-acid dehydratase |
| 3 | 418 | SUPERFAMILY | SSF143975 | IlvD/EDD N-terminal domain-like |
| 3 | 418 | InterPro | IPR037237 | IlvD/EDD, N-terminal domain |
| 2 | 607 | PANTHER | PTHR43661 | D-XYLONATE DEHYDRATASE |
| 507 | 518 | ProSitePatterns | PS00887 | Dihydroxy-acid and 6-phosphogluconate dehydratases signature 2. |
| 507 | 518 | InterPro | IPR020558 | Dihydroxy-acid/6-phosphogluconate dehydratase, conserved site |
| 419 | 570 | Gene3D | G3DSA:3.50.30.80 | - |
| 419 | 570 | InterPro | IPR042096 | Dihydroxy-acid dehydratase, C-terminal |
| 419 | 570 | FunFam | G3DSA:3.50.30.80:FF:000001 | Dihydroxy-acid dehydratase |
| 34 | 603 | Pfam | PF00920 | Dehydratase family |
| 34 | 603 | InterPro | IPR000581 | Dihydroxy-acid/6-phosphogluconate dehydratase |
| 419 | 606 | SUPERFAMILY | SSF52016 | LeuD/IlvD-like |
| 122 | 132 | ProSitePatterns | PS00886 | Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. |
| 122 | 132 | InterPro | IPR020558 | Dihydroxy-acid/6-phosphogluconate dehydratase, conserved site |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA0353
|
AlphaFold | — | — | full sequence | — | Viewing |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 2 | 0.773 |
Ligand evidence
Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| FES | B5ZZ34 | 175.8 Da LogP 1.29 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
S1[Fe]S[Fe]1
|
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
No virtual-screening candidates for this protein.
PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.