Protein profile

KP13_05503

Aspartate-semialdehyde dehydrogenase

Genome: KpKP13

Gene: AHE44509.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GTQ2

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Amino acids 372

Annotations 13

Features 17

PDB binders 4

Druggability 0.838

Overview

Basic information about this protein and its source genome.

Accession: KP13_05503
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE44509.1
Status: annotated
Amino acids: 372
Structure source: AlphaFold + ColabFold

1.2.1.11

GO:0009089 OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate. 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. GO:0009097 OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid. 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:0004073 Catalysis of the reaction: L-aspartate 4-semialdehyde + NADP+ + phosphate = 4-phospho-L-aspartate + H+ + NADPH.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 55.707
DEG E-value: 3.57e-153
Localization: Cytoplasmic
ColabFold pLDDT: 97.26

Selected Druggability evidence

AlphaFold / UniProt model

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 0.838

Structure A0A0H3GTQ2

Pocket Pocket 1

P2Rank 0.76

Structure A0A0H3GTQ2

Pocket Pocket 1

ColabFold model

FPocket 0.418 · Pocket 4

P2Rank 0.681 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 234 / 4744 genomes with a hit

Normalized 0.049

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Enzyme Commission (EC)

1.2.1.11

Gene Ontology (GO)

GO:0009089 OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.
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.
GO:0009097 OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
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: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: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:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
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:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
136	353	Gene3D	G3DSA:3.30.360.10	Dihydrodipicolinate Reductase; domain 2
2	369	NCBIfam	TIGR01745	aspartate-semialdehyde dehydrogenase
2	369	InterPro	IPR011534	Aspartate-semialdehyde dehydrogenase, gamma-type
1	147	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
1	147	InterPro	IPR036291	NAD(P)-binding domain superfamily
3	122	SMART	SM00859	Semialdhyde_dh_3
3	122	InterPro	IPR000534	Semialdehyde dehydrogenase, NAD-binding
144	355	Pfam	PF02774	Semialdehyde dehydrogenase, dimerisation domain
144	355	InterPro	IPR012280	Semialdehyde dehydrogenase, dimerisation domain
262	276	ProSitePatterns	PS01103	Aspartate-semialdehyde dehydrogenase signature.
262	276	InterPro	IPR000319	Aspartate-semialdehyde dehydrogenase, conserved site
134	356	SUPERFAMILY	SSF55347	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
1	372	PIRSF	PIRSF000148	ASA_dh
3	121	Pfam	PF01118	Semialdehyde dehydrogenase, NAD binding domain
3	121	InterPro	IPR000534	Semialdehyde dehydrogenase, NAD-binding
4	358	Gene3D	G3DSA:3.40.50.720	-
2	369	PANTHER	PTHR46278	DEHYDROGENASE, PUTATIVE-RELATED

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

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GTQ2	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_05503	ColabFold	—	—	full sequence	—	Loaded

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				0.838
18				0.599
8				0.244

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	Score	Probability
1	10.83	0.581
2	1.16	0.009
3	0.99	0.005
4	0.83	0.003
5	0.66	0.001

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
4				0.418
15				0.306
14				0.257
2				0.234

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	Score	Probability
1	7.67	0.406
2	1.48	0.02
3	1.39	0.017

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.

55 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	4R5M	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	1PQU	P44801	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
HSE	1PQP	P44801	119.1 Da LogP -1.22 TPSA 83.5	✓ Ro5	✓ Clean	`C(CO)[C@@H](C(=O)O)N`
PEJ	1TB4	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`
ZINC157056	0.656	211.1 Da LogP 0.99 TPSA 117.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1C(=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-])…`
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-]`
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`
ZINC19737412	0.550	234.2 Da LogP 0.87 TPSA 111.2	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1-n1cnnc1`
ZINC2924258	0.550	494.4 Da LogP 3.40 TPSA 219.1	✓ Ro5	✓ Clean	`O=C(Nc1cc([N+](=O)[O-])ccc1C(=O)O)c1ccc(C(=O)Nc…`
ZINC5513707	0.550	331.2 Da LogP 2.45 TPSA 152.7	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1C(=O)Nc1ccc([N+](=O…`
ZINC165626269	0.548	326.1 Da LogP -1.31 TPSA 189.7	1 viol.	✓ Clean	`O=C(O)c1cc(P(=O)(O)O)c(C(=O)O)cc1P(=O)(O)O`
ZINC2523035	0.541	225.2 Da LogP 0.92 TPSA 117.7	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc([N+](=O)[O-])cc1C(=O)O`
ZINC146578839	0.538	246.2 Da LogP -0.06 TPSA 140.6	✓ Ro5	✓ Clean	`NS(=O)(=O)c1cc([N+](=O)[O-])ccc1C(=O)O`
ZINC1621825	0.538	224.2 Da LogP 1.25 TPSA 109.5	✓ Ro5	✓ Clean	`CC(=O)Nc1cc([N+](=O)[O-])ccc1C(=O)O`
ZINC39426455	0.538	225.2 Da LogP 1.08 TPSA 106.7	✓ Ro5	✓ Clean	`COC(=O)c1ccc([N+](=O)[O-])cc1C(=O)O`
ZINC4293805	0.538	271.2 Da LogP 2.52 TPSA 97.5	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1C(=O)c1ccccc1`
ZINC5131766	0.538	224.3 Da LogP -1.26 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)O`
ZINC2840030	0.537	331.2 Da LogP 2.45 TPSA 152.7	✓ Ro5	✓ Clean	`O=C(Nc1cc([N+](=O)[O-])ccc1C(=O)O)c1ccc([N+](=O…`
ZINC285180	0.537	286.2 Da LogP 2.55 TPSA 109.5	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1C(=O)Nc1ccccc1`
ZINC9592202	0.526	288.2 Da LogP 2.87 TPSA 123.6	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1-c1ccc([N+](=O)[O-]…`
ZINC19869585	0.525	255.3 Da LogP 3.18 TPSA 80.4	✓ Ro5	✓ Clean	`CC(C)(C)Sc1ccc([N+](=O)[O-])cc1C(=O)O`
ZINC2159899	0.525	210.1 Da LogP 0.86 TPSA 109.5	✓ Ro5	✓ Clean	`O=CNc1cc([N+](=O)[O-])ccc1C(=O)O`
ZINC1730666	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CSC[C@H](N)C(=O)O)C(=O)O`
ZINC1730667	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSC[C@H](N)C(=O)O)C(=O)O`
ZINC1730669	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSC[C@@H](N)C(=O)O)C(=O)O`
ZINC235386	0.524	286.2 Da LogP 2.55 TPSA 109.5	✓ Ro5	✓ Clean	`O=C(Nc1cc([N+](=O)[O-])ccc1C(=O)O)c1ccccc1`
ZINC3055005	0.524	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	0.524	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	0.524	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC68575534	0.524	224.2 Da LogP 2.11 TPSA 92.5	✓ Ro5	✓ Clean	`CCCNc1cc([N+](=O)[O-])ccc1C(=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.