Overview
Basic information about this protein and its source genome.
- Accession
- PA5084
- Gene
- dadA2 PA5084
- Status
- annotated
- Amino acids
- 416
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- CytoplasmicMembrane
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)
6- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
- GO:0008718 Catalysis of the reaction: a D-alpha-amino acid + a quinone + H2O = a 2-oxocarboxylate + a quinol + NH4+.
- GO:0055130 The chemical reactions and pathways resulting in the breakdown of D-alanine.
- GO:0019478 The chemical reactions and pathways resulting in the breakdown of D-amino acids, the D-enantiomers of amino acids.
- 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 |
|---|---|---|---|---|
| 5 | 54 | Gene3D | G3DSA:3.50.50.60 | - |
| 5 | 54 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
| 4 | 394 | Pfam | PF01266 | FAD dependent oxidoreductase |
| 4 | 394 | InterPro | IPR006076 | FAD dependent oxidoreductase |
| 16 | 20 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 5 | 15 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 137 | 356 | Gene3D | G3DSA:3.30.9.10 | - |
| 4 | 406 | SUPERFAMILY | SSF51905 | FAD/NAD(P)-binding domain |
| 4 | 406 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
| 104 | 396 | Gene3D | G3DSA:3.50.50.60 | - |
| 104 | 396 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
| 267 | 357 | SUPERFAMILY | SSF54373 | FAD-linked reductases, C-terminal domain |
| 21 | 416 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 3 | 396 | PANTHER | PTHR13847 | SARCOSINE DEHYDROGENASE-RELATED |
| 5 | 22 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 1 | 4 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 3 | 408 | Hamap | MF_01202 | D-amino acid dehydrogenase [dadA]. |
| 3 | 408 | InterPro | IPR023080 | D-amino acid dehydrogenase DadA |
| 1 | 20 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
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
PA5084
|
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 | 0.832 | ||||||
| 10 | 0.265 |
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 |
|---|---|---|---|---|---|---|
| B6X | X5IYZ1 | 248.3 Da LogP 2.62 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@H](CC(=O)O)SCC(=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 |
|---|---|---|---|---|---|
| ZINC2377216 | 0.633 | 216.3 Da LogP 2.52 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCCCCC(CC(=O)O)CC(=O)O
|
| ZINC2392141 | 0.600 | 214.3 Da LogP 4.24 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCC(CCCCC)CC(=O)O
|
| ZINC2578862 | 0.594 | 200.3 Da LogP 3.85 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCCC[C@H](CC)CC(=O)O
|
| ZINC59199046 | 0.594 | 200.3 Da LogP 3.85 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCCC[C@@H](CC)CC(=O)O
|
| ZINC100305273 | 0.563 | 286.5 Da LogP 4.91 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCC[C@H](O)CC(=O)O
|
| ZINC100305277 | 0.563 | 286.5 Da LogP 4.91 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCC[C@@H](O)CC(=O)O
|
| ZINC100500540 | 0.563 | 230.3 Da LogP 3.35 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[C@@H](O)CC(=O)O
|
| ZINC100500548 | 0.563 | 258.4 Da LogP 4.13 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[C@H](O)CC(=O)O
|
| ZINC100500553 | 0.563 | 258.4 Da LogP 4.13 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[C@@H](O)CC(=O)O
|
| ZINC16051927 | 0.563 | 216.3 Da LogP 2.96 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC[C@@H](O)CC(=O)O
|
| ZINC2039068 | 0.563 | 244.4 Da LogP 3.74 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCC[C@H](O)CC(=O)O
|
| ZINC2039069 | 0.563 | 244.4 Da LogP 3.74 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCC[C@@H](O)CC(=O)O
|
| ZINC2504625 | 0.563 | 216.3 Da LogP 2.96 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC[C@H](O)CC(=O)O
|
| ZINC2530733 | 0.563 | 200.3 Da LogP 3.85 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@H](C)CC(=O)O
|
| ZINC2558055 | 0.563 | 202.3 Da LogP 2.57 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@H](O)CC(=O)O
|
| ZINC2558056 | 0.563 | 230.3 Da LogP 3.35 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[C@H](O)CC(=O)O
|
| ZINC2578907 | 0.563 | 214.3 Da LogP 4.24 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC[C@H](C)CC(=O)O
|
| ZINC32838984 | 0.563 | 272.4 Da LogP 4.52 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCC[C@@H](O)CC(=O)O
|
| ZINC32838986 | 0.563 | 272.4 Da LogP 4.52 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCC[C@H](O)CC(=O)O
|
| ZINC59297041 | 0.563 | 200.3 Da LogP 3.85 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@@H](C)CC(=O)O
|
| ZINC59658579 | 0.563 | 214.3 Da LogP 4.24 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC[C@@H](C)CC(=O)O
|
| ZINC85915165 | 0.563 | 202.3 Da LogP 2.57 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@@H](O)CC(=O)O
|
| ZINC169110930 | 0.559 | 228.4 Da LogP 4.48 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCCC[C@@H](C)C[C@@H](C)CC(=O)O
|
| ZINC169111027 | 0.559 | 228.4 Da LogP 4.48 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCCC[C@H](C)C[C@@H](C)CC(=O)O
|
| ZINC169111109 | 0.559 | 228.4 Da LogP 4.48 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCCC[C@@H](C)C[C@H](C)CC(=O)O
|
| ZINC169111184 | 0.559 | 228.4 Da LogP 4.48 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CCCCCCC[C@H](C)C[C@H](C)CC(=O)O
|
| ZINC103601590 | 0.545 | 286.4 Da LogP 4.47 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[C@@H](CC(=O)O)C(=O)O
|
| ZINC103601597 | 0.545 | 286.4 Da LogP 4.47 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[C@H](CC(=O)O)C(=O)O
|
| ZINC1603111 | 0.545 | 258.4 Da LogP 3.69 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[C@H](CC(=O)O)C(=O)O
|
| ZINC2027042 | 0.545 | 258.4 Da LogP 3.69 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[C@@H](CC(=O)O)C(=O)O
|
| ZINC2566748 | 0.545 | 202.2 Da LogP 2.13 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@@H](CC(=O)O)C(=O)O
|
| ZINC3199210 | 0.545 | 202.2 Da LogP 2.13 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@H](CC(=O)O)C(=O)O
|
| ZINC1737657 | 0.500 | 238.3 Da LogP 1.75 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCCC(SCC(=O)O)SCC(=O)O
|
| ZINC2839280 | 0.500 | 215.3 Da LogP 1.94 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@@H](CC(=O)O)NC(C)=O
|
| ZINC2839281 | 0.500 | 215.3 Da LogP 1.94 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CCCCCC[C@H](CC(=O)O)NC(C)=O
|
| ZINC38143771 | 0.500 | 260.3 Da LogP 2.27 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@H](C(=O)O)[C@H](O)CC(=O)O
|
| ZINC38143772 | 0.500 | 260.3 Da LogP 2.27 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@@H](C(=O)O)[C@H](O)CC(=O)O
|
| ZINC38143773 | 0.500 | 260.3 Da LogP 2.27 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@H](C(=O)O)[C@@H](O)CC(=O)O
|
| ZINC38143774 | 0.500 | 260.3 Da LogP 2.27 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@@H](C(=O)O)[C@@H](O)CC(=O)O
|
| ZINC72319874 | 0.500 | 288.4 Da LogP 3.05 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[C@H](C(=O)O)[C@H](O)CC(=O)O
|
| ZINC72319875 | 0.500 | 288.4 Da LogP 3.05 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[C@@H](C(=O)O)[C@H](O)CC(=O)O
|
| ZINC72319876 | 0.500 | 288.4 Da LogP 3.05 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[C@H](C(=O)O)[C@@H](O)CC(=O)O
|
| ZINC72319877 | 0.500 | 288.4 Da LogP 3.05 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[C@@H](C(=O)O)[C@@H](O)CC(=O)O
|
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.