Amino acids
370
Annotations
14
Features
18
PDB binders
5
Druggability
0.495
Overview
Basic information about this protein and its source genome.
- Accession
- PA3117
- Gene
- asd PA3117
- Status
- annotated
- Amino acids
- 370
- Structure source
- Experimental + AlphaFold
EC
GO
GO:0004073 Catalysis of the reaction: L-aspartate 4-semialdehyde + NADP+ + phosphate = 4-phospho-L-aspartate + H+ + NADPH.
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:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
GO:0071266 The chemical reactions and pathways resulting in the formation of L-methionine, the L-enantiomer of (2S)-2-amino-4-(methylsulfanyl)butanoic acid, from simpler components such as L-aspartate or L-homoserine. This process occurs in plants, bacteria, archae and fungi.
GO:0019877 OBSOLETE. The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.
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.
FPocket
0.495
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
13 GO
Enzyme Commission (EC)
1Gene Ontology (GO)
13- GO:0004073 Catalysis of the reaction: L-aspartate 4-semialdehyde + NADP+ + phosphate = 4-phospho-L-aspartate + H+ + NADPH.
- 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:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
- GO:0071266 The chemical reactions and pathways resulting in the formation of L-methionine, the L-enantiomer of (2S)-2-amino-4-(methylsulfanyl)butanoic acid, from simpler components such as L-aspartate or L-homoserine. This process occurs in plants, bacteria, archae and fungi.
- GO:0019877 OBSOLETE. The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.
- GO:0009097 OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
- GO:0009089 OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.
- GO:0009088 The chemical reactions and pathways resulting in the formation of L-threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.
- GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
- GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.
- GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
- GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
Sequence Features
Domain/signature hits from InterPro and related databases.
18 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 147 | SUPERFAMILY | SSF51735 | NAD(P)-binding Rossmann-fold domains |
| 1 | 147 | InterPro | IPR036291 | NAD(P)-binding domain superfamily |
| 134 | 355 | SUPERFAMILY | SSF55347 | Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain |
| 2 | 368 | PANTHER | PTHR46278 | DEHYDROGENASE, PUTATIVE-RELATED |
| 136 | 352 | Gene3D | G3DSA:3.30.360.10 | Dihydrodipicolinate Reductase; domain 2 |
| 3 | 122 | SMART | SM00859 | Semialdhyde_dh_3 |
| 3 | 122 | InterPro | IPR000534 | Semialdehyde dehydrogenase, NAD-binding |
| 1 | 368 | Hamap | MF_02121 | Aspartate-semialdehyde dehydrogenase [asd]. |
| 1 | 368 | InterPro | IPR012080 | Aspartate-semialdehyde dehydrogenase |
| 4 | 357 | Gene3D | G3DSA:3.40.50.720 | - |
| 1 | 370 | PIRSF | PIRSF000148 | ASA_dh |
| 3 | 122 | Pfam | PF01118 | Semialdehyde dehydrogenase, NAD binding domain |
| 262 | 276 | ProSitePatterns | PS01103 | Aspartate-semialdehyde dehydrogenase signature. |
| 262 | 276 | InterPro | IPR000319 | Aspartate-semialdehyde dehydrogenase, conserved site |
| 144 | 354 | Pfam | PF02774 | Semialdehyde dehydrogenase, dimerisation domain |
| 144 | 354 | InterPro | IPR012280 | Semialdehyde dehydrogenase, dimerisation domain |
| 2 | 368 | NCBIfam | TIGR01745 | aspartate-semialdehyde dehydrogenase |
| 2 | 368 | InterPro | IPR011534 | Aspartate-semialdehyde dehydrogenase, gamma-type |
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...
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Structural evidence
1 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
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 | 0.495 | ||||||
| 5 | 0.48 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 20.88 | 0.863 | ||||||
| 2 | 3.07 | 0.102 | ||||||
| 3 | 1.68 | 0.028 | ||||||
| 4 | 1.3 | 0.014 |
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 | 0.549 |
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.
56 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 |
|---|---|---|---|---|---|---|
| 4NO | Q9KQG2 | 247.1 Da LogP 0.10 TPSA 138.0 | ✓ Ro5 | ✓ Clean |
c1cc(c(cc1[N+](=O)[O-])P(=O)(O)O)C(=O)O
|
|
| CAC | P44801 | 137.0 Da LogP -0.52 TPSA 40.1 | ✓ Ro5 | ✓ Clean |
C[As](=O)(C)[O-]
|
|
| HSE | P44801 | 119.1 Da LogP -1.22 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
C(CO)[C@@H](C(=O)O)N
|
|
| OEG | P23247 | 134.1 Da LogP -0.83 TPSA 83.8 | ✓ Ro5 | ✓ Clean |
C(C(=O)O)OCC(=O)O
|
|
| PEJ | P44801 | 190.9 Da LogP -7.75 TPSA 92.2 | ✓ Ro5 | ✓ Clean |
[O-]I(=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).
| Ligand | UniProt (homolog) | pchembl | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| CHEMBL457665 | O25801 | 6.75 | 201.2 Da LogP -1.07 TPSA 117.7 | ✓ Ro5 | ✓ Clean |
N[C@@H](CSS(=O)(=O)O)C(=O)O
|
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 |
|---|---|---|---|---|---|
| ZINC1870296 | 1.000 | 247.1 Da LogP 0.10 TPSA 138.0 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc([N+](=O)[O-])cc1P(=O)(O)O
|
| ZINC1870301 | 0.758 | 247.1 Da LogP 0.10 TPSA 138.0 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc([N+](=O)[O-])ccc1P(=O)(O)O
|
| ZINC136105176 | 0.688 | 266.2 Da LogP -0.78 TPSA 111.5 | ✓ Ro5 | ✓ Clean |
O=C(O)COCCOCCOCCOCC(=O)O
|
| ZINC139460448 | 0.688 | 398.4 Da LogP -0.73 TPSA 139.2 | ✓ Ro5 | ✓ Clean |
O=C(O)COCCOCCOCCOCCOCCOCCOCC(=O)O
|
| ZINC143373647 | 0.688 | 486.5 Da LogP -0.69 TPSA 157.7 | 1 viol. | ✓ Clean |
O=C(O)COCCOCCOCCOCCOCCOCCOCCOCCOCC(=O)O
|
| ZINC1542984462 | 0.688 | 442.5 Da LogP -0.71 TPSA 148.4 | ✓ Ro5 | ✓ Clean |
O=C(O)COCCOCCOCCOCCOCCOCCOCCOCC(=O)O
|
| ZINC2584582 | 0.688 | 222.2 Da LogP -0.79 TPSA 102.3 | ✓ Ro5 | ✓ Clean |
O=C(O)COCCOCCOCC(=O)O
|
| ZINC33981097 | 0.688 | 310.3 Da LogP -0.76 TPSA 120.8 | ✓ Ro5 | ✓ Clean |
O=C(O)COCCOCCOCCOCCOCC(=O)O
|
| ZINC34470713 | 0.688 | 354.4 Da LogP -0.74 TPSA 130.0 | ✓ Ro5 | ✓ Clean |
O=C(O)COCCOCCOCCOCCOCCOCC(=O)O
|
| ZINC157056 | 0.656 | 211.1 Da LogP 0.99 TPSA 117.7 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc([N+](=O)[O-])cc1C(=O)O
|
| ZINC3055005 | 0.650 | 204.2 Da LogP -0.63 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O
|
| ZINC3055007 | 0.650 | 204.2 Da LogP -0.63 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC3055010 | 0.650 | 204.2 Da LogP -0.63 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1556249 | 0.636 | 332.2 Da LogP 2.57 TPSA 160.9 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc([N+](=O)[O-])cc1-c1cc([N+](=O)[O-])…
|
| ZINC1555366 | 0.619 | 232.3 Da LogP 0.15 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O
|
| ZINC1555367 | 0.619 | 232.3 Da LogP 0.15 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1555369 | 0.619 | 232.3 Da LogP 0.15 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1720127 | 0.619 | 218.3 Da LogP -0.24 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O
|
| ZINC1720128 | 0.619 | 218.3 Da LogP -0.24 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1720130 | 0.619 | 218.3 Da LogP -0.24 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1764711 | 0.618 | 212.1 Da LogP 1.20 TPSA 123.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc([N+](=O)[O-])cc1[N+](=O)[O-]
|
| ZINC140945368 | 0.611 | 250.2 Da LogP -1.74 TPSA 136.4 | ✓ Ro5 | ✓ Clean |
O=C(O)COC(=O)COCC(=O)OCC(=O)O
|
| ZINC1757911 | 0.600 | 246.0 Da LogP 2.06 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc([N+](=O)[O-])cc1Br
|
| ZINC1870271 | 0.600 | 282.0 Da LogP 1.16 TPSA 100.7 | ✓ Ro5 | ✓ Clean |
O=[N+]([O-])c1ccc(Br)c(P(=O)(O)O)c1
|
| ZINC1870306 | 0.600 | 329.0 Da LogP 1.00 TPSA 100.7 | ✓ Ro5 | ✓ Clean |
O=[N+]([O-])c1ccc(I)c(P(=O)(O)O)c1
|
| ZINC199208276 | 0.600 | 217.1 Da LogP 0.71 TPSA 100.7 | ✓ Ro5 | ✓ Clean |
Cc1ccc([N+](=O)[O-])cc1P(=O)(O)O
|
| ZINC32336 | 0.600 | 201.6 Da LogP 1.95 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc([N+](=O)[O-])cc1Cl
|
| ZINC5427620 | 0.600 | 293.0 Da LogP 1.90 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc([N+](=O)[O-])cc1I
|
| ZINC1717037 | 0.588 | 332.2 Da LogP 2.57 TPSA 160.9 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc([N+](=O)[O-])ccc1-c1ccc([N+](=O)[O-]…
|
| ZINC1870299 | 0.583 | 247.1 Da LogP 0.10 TPSA 138.0 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cccc(P(=O)(O)O)c1[N+](=O)[O-]
|
| ZINC4290726 | 0.583 | 225.2 Da LogP 0.92 TPSA 117.7 | ✓ Ro5 | ✓ Clean |
O=C(O)Cc1cc([N+](=O)[O-])ccc1C(=O)O
|
| ZINC156878 | 0.571 | 201.6 Da LogP 1.95 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc([N+](=O)[O-])ccc1Cl
|
| ZINC4404106 | 0.571 | 212.1 Da LogP 1.20 TPSA 123.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc([N+](=O)[O-])ccc1[N+](=O)[O-]
|
| ZINC19801483 | 0.568 | 223.2 Da LogP 2.59 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
CC(C)(C)c1cc([N+](=O)[O-])ccc1C(=O)O
|
| ZINC2525761 | 0.568 | 235.1 Da LogP 2.31 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc([N+](=O)[O-])cc1C(F)(F)F
|
| ZINC256243285 | 0.568 | 311.0 Da LogP 1.24 TPSA 97.5 | ✓ Ro5 | ✓ Clean |
O=[IH2]c1cc([N+](=O)[O-])ccc1C(=O)O
|
| ZINC1870291 | 0.556 | 217.1 Da LogP 0.71 TPSA 100.7 | ✓ Ro5 | ✓ Clean |
Cc1cc([N+](=O)[O-])ccc1P(=O)(O)O
|
| ZINC2559907 | 0.556 | 293.0 Da LogP 1.90 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc([N+](=O)[O-])ccc1I
|
| ZINC56845 | 0.556 | 246.0 Da LogP 2.06 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc([N+](=O)[O-])ccc1Br
|
| ZINC9592349 | 0.556 | 287.2 Da LogP 2.66 TPSA 117.7 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(-c2ccc([N+](=O)[O-])cc2)cc1C(=O)O
|
| ZINC1587866 | 0.553 | 247.2 Da LogP 0.54 TPSA 134.8 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc([N+](=O)[O-])cc1S(=O)(=O)O
|
| ZINC1870298 | 0.553 | 247.1 Da LogP 0.10 TPSA 138.0 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(P(=O)(O)O)cc1[N+](=O)[O-]
|
| ZINC39151303 | 0.553 | 243.2 Da LogP 2.96 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc([N+](=O)[O-])cc1-c1ccccc1
|
| ZINC59910411 | 0.552 | 217.2 Da LogP -1.13 TPSA 126.9 | ✓ Ro5 | ✓ Clean |
N[C@@H](CSOS(=O)(=O)O)C(=O)O
|
| ZINC112984570 | 0.550 | 398.4 Da LogP -0.17 TPSA 111.1 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCC(=O)O
|
| ZINC1542984426 | 0.550 | 428.5 Da LogP -0.80 TPSA 131.4 | ✓ Ro5 | ✓ Clean |
O=C(O)COCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC167349679 | 0.550 | 442.5 Da LogP -0.15 TPSA 120.4 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCOCC(=O)O
|
| ZINC34249206 | 0.550 | 486.6 Da LogP -0.13 TPSA 129.6 | 1 viol. | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCOCCOCC(=O)O
|
| ZINC38463386 | 0.550 | 354.4 Da LogP -0.18 TPSA 101.9 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCC(=O)O
|
| ZINC39267847 | 0.550 | 208.2 Da LogP -0.89 TPSA 85.2 | ✓ Ro5 | ✓ Clean |
O=C(O)COCCOCCOCCO
|
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.