Protein profile

KP13_00662

Aspartate-semialdehyde dehydrogenase

Genome: KpKP13

Gene: asd AHE42281.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3H447

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Amino acids 368

Annotations 11

Features 21

PDB binders 7

Druggability 0.538

Overview

Basic information about this protein and its source genome.

Accession: KP13_00662
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: asd AHE42281.1
Status: annotated
Amino acids: 368
Structure source: AlphaFold + ColabFold

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 (%): 94.565
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 97.72

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 0.538

Structure A0A0H3H447

Pocket Pocket 1

P2Rank 0.744

Structure A0A0H3H447

Pocket Pocket 1

ColabFold model

FPocket 0.531 · Pocket 1

P2Rank 0.753 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 243 / 4744 genomes with a hit

Normalized 0.051

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

11 GO

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.

Sequence Features

Domain/signature hits from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
1	368	PIRSF	PIRSF000148	ASA_dh
135	355	SUPERFAMILY	SSF55347	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
4	357	Gene3D	G3DSA:3.40.50.720	-
1	368	Hamap	MF_02121	Aspartate-semialdehyde dehydrogenase [asd].
1	368	InterPro	IPR012080	Aspartate-semialdehyde dehydrogenase
262	276	ProSitePatterns	PS01103	Aspartate-semialdehyde dehydrogenase signature.
262	276	InterPro	IPR000319	Aspartate-semialdehyde dehydrogenase, conserved site
4	140	FunFam	G3DSA:3.40.50.720:FF:000152	Aspartate-semialdehyde dehydrogenase
145	354	Pfam	PF02774	Semialdehyde dehydrogenase, dimerisation domain
145	354	InterPro	IPR012280	Semialdehyde dehydrogenase, dimerisation domain
137	352	Gene3D	G3DSA:3.30.360.10	Dihydrodipicolinate Reductase; domain 2
3	123	SMART	SM00859	Semialdhyde_dh_3
3	123	InterPro	IPR000534	Semialdehyde dehydrogenase, NAD-binding
3	121	Pfam	PF01118	Semialdehyde dehydrogenase, NAD binding domain
3	121	InterPro	IPR000534	Semialdehyde dehydrogenase, NAD-binding
2	367	PANTHER	PTHR46278	DEHYDROGENASE, PUTATIVE-RELATED
2	367	NCBIfam	TIGR01745	aspartate-semialdehyde dehydrogenase
2	367	InterPro	IPR011534	Aspartate-semialdehyde dehydrogenase, gamma-type
137	352	FunFam	G3DSA:3.30.360.10:FF:000012	Aspartate-semialdehyde dehydrogenase
1	148	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
1	148	InterPro	IPR036291	NAD(P)-binding domain superfamily

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_A0A0H3H447	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00662	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
5				0.126
8				0.001
2				0.0
6				0.0

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	18.09	0.744
2	2.48	0.055
3	1.75	0.026

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				0.01
3				0.002
5				0.001
10				0.0

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	18.51	0.753
2	2.61	0.061
3	1.48	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.

58 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
3GQ	4R3N	Q8DQ00	210.1 Da LogP 0.78 TPSA 111.9	✓ Ro5	✓ Clean	`c1cc(c(c(c1)C(=O)O)C(=O)O)C(=O)O`
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-]`
DHL	3Q1L	Q8DQ00	77.2 Da LogP -0.13 TPSA 26.0	✓ Ro5	✓ Clean	`C(CS)N`
HSE	1PQP	P44801	119.1 Da LogP -1.22 TPSA 83.5	✓ Ro5	✓ Clean	`C(CO)[C@@H](C(=O)O)N`
OEG	2R00	P23247	134.1 Da LogP -0.83 TPSA 83.8	✓ Ro5	✓ Clean	`C(C(=O)O)OCC(=O)O`
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`
ZINC388710	1.000	210.1 Da LogP 0.78 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)O)c1C(=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`
ZINC133149	0.696	200.6 Da LogP 1.74 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc(Cl)c1C(=O)O`
ZINC134942	0.696	292.0 Da LogP 1.69 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc(I)c1C(=O)O`
ZINC20198570	0.696	245.0 Da LogP 1.85 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc(Br)c1C(=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`
ZINC2040496	0.684	254.1 Da LogP 0.48 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)O)c(C(=O)O)c1C(=O)O`
ZINC5008559	0.682	208.2 Da LogP 1.29 TPSA 91.7	✓ Ro5	✓ Clean	`CC(=O)c1c(C(=O)O)cccc1C(=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`
ZINC1600331	0.650	330.2 Da LogP 2.15 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)O)c1-c1c(C(=O)O)cccc1C(=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-])…`
ZINC45070868	0.619	216.2 Da LogP 2.24 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc2c(C(=O)O)cccc12`
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-]`
ZINC5426383	0.615	234.1 Da LogP 2.10 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(F)(F)F)c1C(=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`
ZINC3209425	0.593	223.2 Da LogP 1.04 TPSA 103.7	✓ Ro5	✓ Clean	`CC(=O)Nc1cccc(C(=O)O)c1C(=O)O`
ZINC1559267	0.591	292.0 Da LogP 1.69 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)O)c1I`
ZINC3158512	0.591	245.0 Da LogP 1.85 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)O)c1Br`
ZINC6750304	0.591	200.6 Da LogP 1.74 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)O)c1Cl`
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-]…`
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`
ZINC1677584	0.571	224.2 Da LogP 0.57 TPSA 129.7	✓ Ro5	✓ Clean	`NC(=O)Nc1cccc(C(=O)O)c1C(=O)O`
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-]`
ZINC4428360	0.571	298.2 Da LogP 0.18 TPSA 186.5	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)O)c(C(=O)O)c1C(=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`
ZINC134881	0.565	216.2 Da LogP 2.24 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc2cccc(C(=O)O)c12`
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`
ZINC34929195	0.552	233.2 Da LogP 0.66 TPSA 105.3	✓ Ro5	✓ Clean	`O=C(O)c1cccc(-n2cnnc2)c1C(=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.