Amino acids
298
Annotations
7
Features
19
PDB binders
9
Druggability
0.814
Overview
Basic information about this protein and its source genome.
- Accession
- PA3569
- Gene
- mmsB PA3569
- Status
- annotated
- Amino acids
- 298
- Structure source
- AlphaFold
EC
GO
GO:0008442 Catalysis of the reaction: 3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0006574 The chemical reactions and pathways resulting in the breakdown of L-valine.
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.
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 48.235
- Human E-value
- 2.5000000000000002e-48
- 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.
FPocket
0.814
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
6 GO
Enzyme Commission (EC)
1Gene Ontology (GO)
6- GO:0008442 Catalysis of the reaction: 3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+.
- GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
- GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
- GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
- GO:0006574 The chemical reactions and pathways resulting in the breakdown of L-valine.
- 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.
19 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 165 | 293 | Pfam | PF14833 | NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase |
| 165 | 293 | InterPro | IPR029154 | 3-hydroxyisobutyrate dehydrogenase-like, NAD-binding domain |
| 165 | 298 | Gene3D | G3DSA:1.10.1040.10 | - |
| 165 | 298 | InterPro | IPR013328 | 6-phosphogluconate dehydrogenase, domain 2 |
| 2 | 163 | SUPERFAMILY | SSF51735 | NAD(P)-binding Rossmann-fold domains |
| 2 | 163 | InterPro | IPR036291 | NAD(P)-binding domain superfamily |
| 1 | 297 | PIRSF | PIRSF000103 | HIBADH |
| 1 | 297 | InterPro | IPR015815 | 3-hydroxyisobutyrate dehydrogenase-related |
| 6 | 295 | NCBIfam | TIGR01692 | 3-hydroxyisobutyrate dehydrogenase |
| 6 | 295 | InterPro | IPR011548 | 3-hydroxyisobutyrate dehydrogenase |
| 2 | 295 | PANTHER | PTHR22981 | 3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED |
| 163 | 296 | SUPERFAMILY | SSF48179 | 6-phosphogluconate dehydrogenase C-terminal domain-like |
| 163 | 296 | InterPro | IPR008927 | 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily |
| 165 | 298 | FunFam | G3DSA:1.10.1040.10:FF:000006 | 3-hydroxyisobutyrate dehydrogenase |
| 3 | 162 | Pfam | PF03446 | NAD binding domain of 6-phosphogluconate dehydrogenase |
| 3 | 162 | InterPro | IPR006115 | 6-phosphogluconate dehydrogenase, NADP-binding |
| 6 | 19 | ProSitePatterns | PS00895 | 3-hydroxyisobutyrate dehydrogenase signature. |
| 6 | 19 | InterPro | IPR002204 | 3-hydroxyisobutyrate dehydrogenase-related, conserved site |
| 1 | 164 | Gene3D | G3DSA:3.40.50.720 | - |
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...
Legend
High
Medium
Low
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
PA3569
|
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 | 0.814 |
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.
59 records
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 |
|---|---|---|---|---|---|---|
| 3OH | P9WNY5 | 90.1 Da LogP -0.55 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
C(CO)C(=O)O
|
|
| 7VD | I6R485 | 138.1 Da LogP -0.25 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CC(=O)CP(=O)(O)O
|
|
| 9ON | P9WNY5 | 146.1 Da LogP 0.57 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@@H](CCC(=O)O)C(=O)O
|
|
| AKR | P9WNY5 | 72.1 Da LogP 0.26 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
C=CC(=O)O
|
|
| BO3 | P0A9V8 | 61.8 Da LogP -2.05 TPSA 60.7 | ✓ Ro5 | ✓ Clean |
B(O)(O)O
|
|
| HIU | P9WNY5 | 104.1 Da LogP -0.30 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
C[C@H](CO)C(=O)O
|
|
| HUI | P9WNY5 | 104.1 Da LogP -0.30 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
C[C@@H](CO)C(=O)O
|
|
| LLQ | P0A9V8 | 156.2 Da LogP -1.77 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
C([C@@H](CS(=O)(=O)O)O)O
|
|
| TLA | A3MU08 | 150.1 Da LogP -2.12 TPSA 115.1 | ✓ Ro5 | ✓ Clean |
[C@@H]([C@H](C(=O)O)O)(C(=O)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 |
|---|---|---|---|---|---|
| ZINC12359024 | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O
|
| ZINC13533920 | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC1532740 | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O
|
| ZINC1549593 | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC2013424 | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O
|
| ZINC3581021 | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC3860635 | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O
|
| ZINC5783661 | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O
|
| ZINC6072527 | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC2029340 | 0.591 | 216.3 Da LogP 2.38 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@@H](CCCCC[C@@H](C)C(=O)O)C(=O)O
|
| ZINC2029341 | 0.591 | 216.3 Da LogP 2.38 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@H](CCCCC[C@@H](C)C(=O)O)C(=O)O
|
| ZINC2029343 | 0.591 | 216.3 Da LogP 2.38 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@@H](CCCCC[C@H](C)C(=O)O)C(=O)O
|
| ZINC2029346 | 0.591 | 230.3 Da LogP 2.77 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@@H](CCCCCC[C@@H](C)C(=O)O)C(=O)O
|
| ZINC2029348 | 0.591 | 230.3 Da LogP 2.77 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@H](CCCCCC[C@@H](C)C(=O)O)C(=O)O
|
| ZINC2029350 | 0.591 | 230.3 Da LogP 2.77 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@@H](CCCCCC[C@H](C)C(=O)O)C(=O)O
|
| ZINC2029355 | 0.591 | 258.4 Da LogP 3.55 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@@H](CCCCCCCC[C@@H](C)C(=O)O)C(=O)O
|
| ZINC2029358 | 0.591 | 258.4 Da LogP 3.55 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@H](CCCCCCCC[C@@H](C)C(=O)O)C(=O)O
|
| ZINC2029360 | 0.591 | 258.4 Da LogP 3.55 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@@H](CCCCCCCC[C@H](C)C(=O)O)C(=O)O
|
| ZINC4100991 | 0.591 | 286.4 Da LogP 4.33 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@@H](CCCCCCCCCC[C@@H](C)C(=O)O)C(=O)O
|
| ZINC4100995 | 0.591 | 286.4 Da LogP 4.33 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@H](CCCCCCCCCC[C@@H](C)C(=O)O)C(=O)O
|
| ZINC4101001 | 0.591 | 286.4 Da LogP 4.33 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[C@@H](CCCCCCCCCC[C@H](C)C(=O)O)C(=O)O
|
| ZINC1560405156 | 0.588 | 208.1 Da LogP -1.79 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O
|
| ZINC1560405157 | 0.588 | 208.1 Da LogP -1.79 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O
|
| ZINC142127993 | 0.571 | 219.2 Da LogP -1.20 TPSA 123.9 | ✓ Ro5 | ✓ Clean |
C[C@H](O)C(=O)N[C@@H](CCC(=O)O)C(=O)O
|
| ZINC214811896 | 0.571 | 219.2 Da LogP -1.20 TPSA 123.9 | ✓ Ro5 | ✓ Clean |
C[C@@H](O)C(=O)N[C@@H](CCC(=O)O)C(=O)O
|
| ZINC214811946 | 0.571 | 219.2 Da LogP -1.20 TPSA 123.9 | ✓ Ro5 | ✓ Clean |
C[C@H](O)C(=O)N[C@H](CCC(=O)O)C(=O)O
|
| ZINC214811999 | 0.571 | 219.2 Da LogP -1.20 TPSA 123.9 | ✓ Ro5 | ✓ Clean |
C[C@@H](O)C(=O)N[C@H](CCC(=O)O)C(=O)O
|
| ZINC13529664 | 0.560 | 320.3 Da LogP -1.08 TPSA 190.3 | 1 viol. | ✓ Clean |
O=C(O)CC[C@H](NC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=…
|
| ZINC14510370 | 0.556 | 244.4 Da LogP 3.74 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCCCCO
|
| ZINC1531061 | 0.556 | 216.3 Da LogP 2.96 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCCO
|
| ZINC1610426 | 0.556 | 230.3 Da LogP 3.35 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCCCO
|
| ZINC2168567 | 0.556 | 202.3 Da LogP 2.57 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCO
|
| ZINC3861297 | 0.556 | 272.4 Da LogP 4.52 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCCCCCCO
|
| ZINC4284502 | 0.556 | 258.4 Da LogP 4.13 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCCCCCO
|
| ZINC5287109 | 0.556 | 286.5 Da LogP 4.91 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCCCCCCCO
|
| ZINC2242980 | 0.552 | 218.2 Da LogP -1.23 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
C[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O
|
| ZINC2560662 | 0.552 | 218.2 Da LogP -1.23 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
C[C@@H](N)C(=O)N[C@H](CCC(=O)O)C(=O)O
|
| ZINC5360219 | 0.552 | 231.2 Da LogP 0.47 TPSA 103.7 | ✓ Ro5 | ✓ Clean |
CC(C)CC(=O)N[C@@H](CCC(=O)O)C(=O)O
|
| ZINC3845741 | 0.542 | 202.2 Da LogP 1.84 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CC(C)[C@@H](CC[C@@H](C)C(=O)O)C(=O)O
|
| ZINC3845742 | 0.542 | 202.2 Da LogP 1.84 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CC(C)[C@H](CC[C@@H](C)C(=O)O)C(=O)O
|
| ZINC3845743 | 0.542 | 202.2 Da LogP 1.84 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CC(C)[C@@H](CC[C@H](C)C(=O)O)C(=O)O
|
| ZINC3845744 | 0.542 | 202.2 Da LogP 1.84 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CC(C)[C@H](CC[C@H](C)C(=O)O)C(=O)O
|
| ZINC217513646 | 0.538 | 362.3 Da LogP -1.76 TPSA 207.4 | 1 viol. | ✓ Clean |
O=C(O)CC[C@H](NC(=O)CC(=O)N[C@@H](CCC(=O)O)C(=O…
|
| ZINC225956904 | 0.538 | 362.3 Da LogP -1.76 TPSA 207.4 | 1 viol. | ✓ Clean |
O=C(O)CC[C@H](NC(=O)CC(=O)N[C@H](CCC(=O)O)C(=O)…
|
| ZINC225956918 | 0.538 | 362.3 Da LogP -1.76 TPSA 207.4 | 1 viol. | ✓ Clean |
O=C(O)CC[C@@H](NC(=O)CC(=O)N[C@H](CCC(=O)O)C(=O…
|
| ZINC58123315 | 0.538 | 376.3 Da LogP -1.36 TPSA 207.4 | 1 viol. | ✓ Clean |
O=C(O)CC[C@H](NC(=O)CCC(=O)N[C@@H](CCC(=O)O)C(=…
|
| ZINC58123320 | 0.538 | 376.3 Da LogP -1.36 TPSA 207.4 | 1 viol. | ✓ Clean |
O=C(O)CC[C@H](NC(=O)CCC(=O)N[C@H](CCC(=O)O)C(=O…
|
| ZINC58123326 | 0.538 | 376.3 Da LogP -1.36 TPSA 207.4 | 1 viol. | ✓ Clean |
O=C(O)CC[C@@H](NC(=O)CCC(=O)N[C@H](CCC(=O)O)C(=…
|
| ZINC87491353 | 0.536 | 259.3 Da LogP -3.16 TPSA 138.5 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)C[C@@H](O)CN(CO)C(CO)CO
|
| ZINC87491354 | 0.536 | 259.3 Da LogP -3.16 TPSA 138.5 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)C[C@H](O)CN(CO)C(CO)CO
|
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.