Overview
Basic information about this protein and its source genome.
- Accession
- PA2003
- Gene
- PA2003 bdhA
- Status
- annotated
- Amino acids
- 256
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 40.323
- Human E-value
- 4.6e-07
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- 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.
MTLKGKTALVTGSTSGIGLGIALSLAEAGADLLLNGFGEVDAALAQVRARGVRAEHHPADLSSPEQIGELMAFAERTFGGVDILVNNAGIQYVAPVQEFPTERWDAIIAINLSSVFHTTRLALPGMLARGWGRIVNIASTHGLVASAGKSAYVAAKHGVLGLTKSVALETARTPVTCNAICPGWVLTPLVQKQIDARTAEGVSPEQAEHDLLAEKQPSLAFVTPEQLGGLTLFLCSEAADQVRGAAWNMDGGWVAQ
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
4- GO:0003858 Catalysis of the reaction: (R)-3-hydroxybutanoate + NAD+ = acetoacetate + H+ + NADH.
- GO:0016628 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces NAD or NADP.
- GO:0032787 The chemical reactions and pathways involving monocarboxylic acids, any organic acid containing one carboxyl (COOH) group or anion (COO-).
- GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 7 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 79 | 90 | PRINTS | PR00080 | Short-chain dehydrogenase/reductase (SDR) superfamily signature |
| 79 | 90 | InterPro | IPR002347 | Short-chain dehydrogenase/reductase SDR |
| 132 | 140 | PRINTS | PR00080 | Short-chain dehydrogenase/reductase (SDR) superfamily signature |
| 132 | 140 | InterPro | IPR002347 | Short-chain dehydrogenase/reductase SDR |
| 152 | 171 | PRINTS | PR00080 | Short-chain dehydrogenase/reductase (SDR) superfamily signature |
| 152 | 171 | InterPro | IPR002347 | Short-chain dehydrogenase/reductase SDR |
| 1 | 255 | SUPERFAMILY | SSF51735 | NAD(P)-binding Rossmann-fold domains |
| 1 | 255 | InterPro | IPR036291 | NAD(P)-binding domain superfamily |
| 6 | 195 | Pfam | PF00106 | short chain dehydrogenase |
| 6 | 195 | InterPro | IPR002347 | Short-chain dehydrogenase/reductase SDR |
| 139 | 167 | ProSitePatterns | PS00061 | Short-chain dehydrogenases/reductases family signature. |
| 139 | 167 | InterPro | IPR020904 | Short-chain dehydrogenase/reductase, conserved site |
| 1 | 26 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 1 | 256 | FunFam | G3DSA:3.40.50.720:FF:000084 | Short-chain dehydrogenase reductase |
| 20 | 26 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 27 | 256 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 79 | 90 | PRINTS | PR00081 | Glucose/ribitol dehydrogenase family signature |
| 152 | 171 | PRINTS | PR00081 | Glucose/ribitol dehydrogenase family signature |
| 7 | 24 | PRINTS | PR00081 | Glucose/ribitol dehydrogenase family signature |
| 7 | 24 | InterPro | IPR002347 | Short-chain dehydrogenase/reductase SDR |
| 173 | 190 | PRINTS | PR00081 | Glucose/ribitol dehydrogenase family signature |
| 173 | 190 | InterPro | IPR002347 | Short-chain dehydrogenase/reductase SDR |
| 217 | 237 | PRINTS | PR00081 | Glucose/ribitol dehydrogenase family signature |
| 217 | 237 | InterPro | IPR002347 | Short-chain dehydrogenase/reductase SDR |
| 126 | 142 | PRINTS | PR00081 | Glucose/ribitol dehydrogenase family signature |
| 126 | 142 | InterPro | IPR002347 | Short-chain dehydrogenase/reductase SDR |
| 1 | 256 | Gene3D | G3DSA:3.40.50.720 | - |
| 8 | 19 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 1 | 255 | PANTHER | PTHR42879 | 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE |
| 6 | 256 | NCBIfam | TIGR01963 | 3-hydroxybutyrate dehydrogenase |
| 6 | 256 | InterPro | IPR011294 | 3-hydroxybutyrate dehydrogenase |
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
PA2003
|
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.707 | ||||||
| 2 | 0.223 |
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 |
|---|---|---|---|---|---|---|
| 1PS | Q5P8S7 | 201.2 Da LogP -0.09 TPSA 61.1 | ✓ Ro5 | ✓ Clean |
c1cc[n+](cc1)CCCS(=O)(=O)[O-]
|
|
| 3HL | Q5KST5 | 104.1 Da LogP -0.16 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
C[C@@H](CC(=O)O)O
|
|
| 3HR | D0VWQ0 | 104.1 Da LogP -0.16 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
C[C@H](CC(=O)O)O
|
|
| AAE | A0A1E3M3N6 | 102.1 Da LogP 0.05 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CC(=O)CC(=O)O
|
|
| DXX | D0VWQ0 | 118.1 Da LogP -0.21 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CC(C(=O)O)C(=O)O
|
|
| MLA | D0VWQ0 | 104.1 Da LogP -0.45 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C(C(=O)O)C(=O)O
|
|
| QT8 | A0A1E3M3N6 | 116.1 Da LogP 0.44 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCC(=O)CC(=O)O
|
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).
| Ligand | Tanimoto | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|
| ZINC4521819 | 0.643 | 202.3 Da LogP 0.25 TPSA 58.3 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCC[n+]1ccccc1
|
| ZINC4831627 | 0.593 | 370.5 Da LogP -0.21 TPSA 76.0 | ✓ Ro5 | ✓ Clean |
O=S(=O)(CC[n+]1ccccc1)CCS(=O)(=O)CC[n+]1ccccc1
|
| ZINC22112620 | 0.567 | 216.3 Da LogP 0.64 TPSA 58.3 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCCC[n+]1ccccc1
|
| ZINC13546016 | 0.560 | 276.3 Da LogP 0.49 TPSA 110.1 | ✓ Ro5 | ✓ Clean |
C[C@H](O)CC(=O)O[C@@H](C)CC(=O)O[C@@H](C)CC(=O)O
|
| ZINC13546018 | 0.560 | 276.3 Da LogP 0.49 TPSA 110.1 | ✓ Ro5 | ✓ Clean |
C[C@H](O)CC(=O)O[C@H](C)CC(=O)O[C@@H](C)CC(=O)O
|
| ZINC257400894 | 0.560 | 276.3 Da LogP 0.49 TPSA 110.1 | ✓ Ro5 | ✓ Clean |
C[C@H](O)CC(=O)O[C@H](C)CC(=O)O[C@H](C)CC(=O)O
|
| ZINC257400895 | 0.560 | 276.3 Da LogP 0.49 TPSA 110.1 | ✓ Ro5 | ✓ Clean |
C[C@H](O)CC(=O)O[C@@H](C)CC(=O)O[C@H](C)CC(=O)O
|
| ZINC1634282 | 0.542 | 214.3 Da LogP 1.74 TPSA 7.8 | ✓ Ro5 | ✓ Clean |
c1cc[n+](CCCC[n+]2ccccc2)cc1
|
| ZINC390794 | 0.542 | 200.3 Da LogP 1.35 TPSA 7.8 | ✓ Ro5 | ✓ Clean |
c1cc[n+](CCC[n+]2ccccc2)cc1
|
| ZINC1668279 | 0.520 | 228.3 Da LogP 2.13 TPSA 7.8 | ✓ Ro5 | ✓ Clean |
c1cc[n+](CCCCC[n+]2ccccc2)cc1
|
| ZINC1669613 | 0.520 | 298.5 Da LogP 4.08 TPSA 7.8 | ✓ Ro5 | ✓ Clean |
c1cc[n+](CCCCCCCCCC[n+]2ccccc2)cc1
|
| ZINC5583130 | 0.520 | 242.4 Da LogP 2.52 TPSA 7.8 | ✓ Ro5 | ✓ Clean |
c1cc[n+](CCCCCC[n+]2ccccc2)cc1
|
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.