KpATCC43816 Protein target profile

glutamate dehydrogenase

Accession: VK055_1018

Gene: gdhA AIK79641.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A060VIF0

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Length 424

Pocket druggability (P2Rank · AlphaFold DB model) 0.956

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 58 total records

Functional annotation 0 EC 7 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.96. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 6 structural and 2 bioactivity records.

Risks to review

Evidence coverage

Core evidence streams are available for this target.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 49.333 Lower values reduce human off-target concern.
Human E-value: 2.32e-20
Gut microbiome similarity: 1.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 64.678 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.93 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.956

Structure A0A060VIF0

Pocket Pocket 1

Druggability (FPocket) 0.151

Structure A0A060VIF0

Pocket Pocket 23

ColabFold model

P2Rank 0.947 · Pocket 1

FPocket 0.255 · Pocket 21

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 84 / 4744 genomes with a hit

Prevalence 1.8%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MEKLSYASESSTSPWTTYLRQIDRVAPYLGDLAYWVETLRHPKRALIVDIPVQMDDGTIRHFEGYRVQHNLSRGPGKGGVRYHPDVDLNEVMALSAWMTIKCAAVNIPYGGAKGGIRVDPFSLSEGELERLTRRYTSEIGIIIGPQKDIPAPDVGTNGKVMAWMMDTYSMNHGTTITGVVTGKPIHLGGSLGREKATGRGVFVTGREVARRAGIEIEGAKVALQGFGNVGSEAARLFAGVGARIVVIQDHTATLYNEGGIDMAALTAWQAEKKQIAGFPGAQEIDKDAFWTTPMDILIPAALEGQITRERAEKLTCKLVLEGANGPTYPEADDVLAERGVIVVPDVICNAGGVTVSYFEWVQDMASFFWSEEEINAKMDRIMTDAIVHVWDKAAEKECTLRTAAYIVACERILMARKDRGIYPG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
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.
GO:0016639 Catalysis of an oxidation-reduction (redox) reaction in which a CH-NH2 group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0004352 Catalysis of the reaction: L-glutamate + NAD+ + H2O = 2-oxoglutarate + NH4+ + NADH + H+.
GO:0004354 Catalysis of the reaction: L-glutamate + NADP+ + H2O = 2-oxoglutarate + NH4+ + NADPH + H+.
GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
GO:0006538 The chemical reactions and pathways resulting in the breakdown of L-glutamate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

30 records

Show feature table

Start	End	DB	Term	Name
10	190	SUPERFAMILY	SSF53223	Aminoacid dehydrogenase-like, N-terminal domain
10	190	InterPro	IPR046346	Aminoacid dehydrogenase-like, N-terminal domain superfamily
190	420	SMART	SM00839	ELFV_dehydrog_3
190	420	InterPro	IPR006096	Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal
188	412	CDD	cd01076	NAD_bind_1_Glu_DH
188	412	InterPro	IPR033922	NAD(P) binding domain of glutamate dehydrogenase
3	350	Gene3D	G3DSA:1.10.8.1210	-
44	187	FunFam	G3DSA:3.40.50.10860:FF:000003	Glutamate dehydrogenase
188	420	Pfam	PF00208	Glutamate/Leucine/Phenylalanine/Valine dehydrogenase
188	420	InterPro	IPR006096	Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal
42	170	Pfam	PF02812	Glu/Leu/Phe/Val dehydrogenase, dimerisation domain
42	170	InterPro	IPR006097	Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain
188	423	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
188	423	InterPro	IPR036291	NAD(P)-binding domain superfamily
195	349	Gene3D	G3DSA:3.40.50.720	-
221	241	PRINTS	PR00082	Glutamate/leucine/phenylalanine/valine dehydrogenase signature
221	241	InterPro	IPR006095	Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase
179	201	PRINTS	PR00082	Glutamate/leucine/phenylalanine/valine dehydrogenase signature
179	201	InterPro	IPR006095	Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase
99	113	PRINTS	PR00082	Glutamate/leucine/phenylalanine/valine dehydrogenase signature
99	113	InterPro	IPR006095	Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase
348	359	PRINTS	PR00082	Glutamate/leucine/phenylalanine/valine dehydrogenase signature
348	359	InterPro	IPR006095	Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase
9	423	PIRSF	PIRSF000185	Glu_DH
9	423	InterPro	IPR014362	Glutamate dehydrogenase
12	415	PANTHER	PTHR11606	GLUTAMATE DEHYDROGENASE
376	423	Gene3D	G3DSA:1.10.8.1210	-
40	175	Gene3D	G3DSA:3.40.50.10860	Leucine Dehydrogenase, chain A, domain 1
107	120	ProSitePatterns	PS00074	Glu / Leu / Phe / Val dehydrogenases active site.
107	120	InterPro	IPR033524	Leu/Phe/Val dehydrogenases active site

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.956

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Surrounding area

Pocket 2 P2Rank #2

0.08

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Surrounding area

Pocket 3 P2Rank #3

0.046

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Surrounding area

Pocket 4 P2Rank #4

0.019

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Surrounding area

Pocket 5 P2Rank #5

0.004

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.947

Likely same site as FPocket 23 2.5 Å 38 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.076

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Surrounding area

Pocket 3 P2Rank #3

0.056

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Surrounding area

Pocket 4 P2Rank #4

0.034

Likely same site as FPocket 21 1.6 Å 11 shared residues 100% of smaller site

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #21

0.255

Likely same site as P2Rank 4 1.6 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #23

0.219 Unusual size

Likely same site as P2Rank 1 2.5 Å 38 shared residues 100% of smaller site

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A060VIF0	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1018	ColabFold	—	—	full sequence	—	Loaded

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

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AKG PDB via homolog 146.1 Da · LogP -0.50 · TPSA 91.7 Open detail RCSB PDB

B1T PDB via homolog Detail RCSB PDB

GWD PDB via homolog Detail RCSB PDB

H3P PDB via homolog Detail RCSB PDB

NH4 PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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
AKG RCSB PDB	1HWY	P00366	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
B1T RCSB PDB	3ETD	P00366	356.1 Da LogP 5.86 TPSA 40.5	1 viol.	✓ Clean	`c1c(cc(c(c1Sc2cc(cc(c2O)Cl)Cl)O)Cl)Cl`
GWD RCSB PDB	3ETG	P00366	520.9 Da LogP 5.01 TPSA 49.3	2 viol.	✓ Clean	`c1cc2c(cc1I)/C(=C\c3cc(c(c(c3)Br)O)Br)/C(=O)N2`
H3P RCSB PDB	3ETE	P00366	406.9 Da LogP 6.61 TPSA 40.5	1 viol.	✓ Clean	`c1c(c(c(c(c1Cl)Cl)Cc2c(c(cc(c2Cl)Cl)Cl)O)O)Cl`
NH4 RCSB PDB	3AOG	Q72IC1	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
XEG RCSB PDB	6DHL	P00366	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`c1cc(c(cc1[C@@H]2[C@H](Cc3c(cc(cc3O2)O)O)OC(=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
CHEMBL3400559 ChEMBL	P00366	—	817.5 Da LogP 1.07 TPSA 345.0	3 viol.	✓ Clean	`C/C(=C\c1ccc(C2(C(F)(F)F)N=N2)cc1O)C(=O)NCCNP(=…`
CHEMBL3400560 ChEMBL	P00366	—	737.5 Da LogP 0.96 TPSA 298.5	3 viol.	✓ Clean	`C/C(=C\c1ccc(C2(C(F)(F)F)N=N2)cc1O)C(=O)NCCNP(=…`

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
ZINC3978503 ZINC	1.000	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)…`
ZINC4534390 ZINC	1.000	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)c…`
ZINC4544252 ZINC	1.000	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c1…`
ZINC8681494 ZINC	1.000	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c…`
ZINC3870412 ZINC	0.851	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c…`
ZINC3870413 ZINC	0.851	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(…`
ZINC3870414 ZINC	0.851	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c(…`
ZINC3870415 ZINC	0.851	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(O…`
ZINC14642643 ZINC	0.849	456.4 Da LogP 2.83 TPSA 166.1	1 viol.	Alert	`COc1cc(C(=O)O[C@@H]2Cc3c(O)cc(O)cc3O[C@@H]2c2cc…`
ZINC14727965 ZINC	0.837	426.4 Da LogP 2.82 TPSA 156.9	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)cc1)…`
ZINC3843497 ZINC	0.762	370.0 Da LogP 4.71 TPSA 80.9	✓ Ro5	✓ Clean	`Oc1c(Cl)cc(Cl)c(O)c1Cc1c(O)c(Cl)cc(Cl)c1O`
ZINC14436185 ZINC	0.741	472.4 Da LogP 2.54 TPSA 186.4	2 viol.	Alert	`COc1cc(C(=O)O[C@@H]2Cc3c(O)cc(O)cc3O[C@@H]2c2cc…`
ZINC21992193 ZINC	0.722	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c…`
ZINC21992196 ZINC	0.722	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c(…`
ZINC21992198 ZINC	0.722	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(…`
ZINC21992201 ZINC	0.722	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(O…`
ZINC1903857763 ZINC	0.689	411.0 Da LogP 4.12 TPSA 69.6	✓ Ro5	Alert	`O=C1Nc2ccc(Br)cc2C1=Cc1cc(O)c(O)c(Br)c1`
ZINC2104376 ZINC	0.689	411.0 Da LogP 4.12 TPSA 69.6	✓ Ro5	Alert	`O=C1Nc2ccc(Br)cc2/C1=C/c1cc(O)c(O)c(Br)c1`
ZINC96481959 ZINC	0.689	411.0 Da LogP 4.12 TPSA 69.6	✓ Ro5	Alert	`O=C1Nc2ccc(Br)cc2/C1=C\c1cc(O)c(O)c(Br)c1`
ZINC14642853 ZINC	0.632	442.4 Da LogP 2.18 TPSA 177.1	1 viol.	Alert	`O=C(Oc1cc(O)cc2c1C[C@H](O)[C@@H](c1ccc(O)c(O)c1…`
ZINC15016062 ZINC	0.620	425.1 Da LogP 4.42 TPSA 58.6	✓ Ro5	✓ Clean	`COc1cc(/C=C2\C(=O)Nc3ccc(Br)cc32)cc(Br)c1O`
ZINC13610584 ZINC	0.619	498.5 Da LogP 2.89 TPSA 177.1	1 viol.	Alert	`O=C(C[C@H](O)CCc1ccc(O)c(O)c1)O[C@@H]1Cc2c(O)cc…`
ZINC13610587 ZINC	0.619	498.5 Da LogP 2.89 TPSA 177.1	1 viol.	Alert	`O=C(C[C@@H](O)CCc1ccc(O)c(O)c1)O[C@H]1Cc2c(O)cc…`
ZINC13610590 ZINC	0.619	498.5 Da LogP 2.89 TPSA 177.1	1 viol.	Alert	`O=C(C[C@H](O)CCc1ccc(O)c(O)c1)O[C@H]1Cc2c(O)cc(…`
ZINC8652640 ZINC	0.619	498.5 Da LogP 2.89 TPSA 177.1	1 viol.	Alert	`O=C(C[C@@H](O)CCc1ccc(O)c(O)c1)O[C@@H]1Cc2c(O)c…`
ZINC119978 ZINC	0.600	290.3 Da LogP 1.55 TPSA 110.4	✓ Ro5	Alert	`Oc1cc(O)c2c(c1)O[C@@H](c1ccc(O)c(O)c1)[C@@H](O)…`
ZINC119983 ZINC	0.600	290.3 Da LogP 1.55 TPSA 110.4	✓ Ro5	Alert	`Oc1cc(O)c2c(c1)O[C@H](c1ccc(O)c(O)c1)[C@@H](O)C2`
ZINC119985 ZINC	0.600	290.3 Da LogP 1.55 TPSA 110.4	✓ Ro5	Alert	`Oc1cc(O)c2c(c1)O[C@@H](c1ccc(O)c(O)c1)[C@H](O)C2`
ZINC119988 ZINC	0.600	290.3 Da LogP 1.55 TPSA 110.4	✓ Ro5	Alert	`Oc1cc(O)c2c(c1)O[C@H](c1ccc(O)c(O)c1)[C@H](O)C2`
ZINC1569727 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC1569728 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC1569729 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC1569730 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC1560407548 ZINC	0.586	441.4 Da LogP 2.69 TPSA 177.1	1 viol.	Alert	`O=C(O[C]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)c1)…`
ZINC2522597 ZINC	0.586	246.3 Da LogP -0.60 TPSA 129.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)C[C@H](N)C(=O)O)C(=O)O`
ZINC5567094 ZINC	0.585	390.0 Da LogP 1.67 TPSA 95.5	✓ Ro5	Alert	`O=C1NC(=O)C(=Cc2cc(Br)c(O)c(Br)c2)C(=O)N1`
ZINC1532219 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)O`
ZINC1532220 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](N)CC(C)C)C(=O)O`
ZINC1532221 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@H](CC(C)C)C(=O)O`
ZINC1532222 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@H](CC(C)C)C(=O)O`
ZINC394419 ZINC	0.565	231.9 Da LogP 4.01 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1c(Cl)cc(Cl)c(Cl)c1Cl`
ZINC15016055 ZINC	0.560	376.2 Da LogP 3.66 TPSA 67.8	✓ Ro5	✓ Clean	`COc1cc(/C=C2\C(=O)Nc3ccc(Br)cc32)cc(OC)c1O`
ZINC59426354 ZINC	0.558	406.1 Da LogP 1.83 TPSA 78.4	✓ Ro5	Alert	`O=C1NC(=S)NC(=O)C1=Cc1cc(Br)c(O)c(Br)c1`
ZINC1605717 ZINC	0.552	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@H](C(=O)O)C(C)C`
ZINC1605718 ZINC	0.552	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@H](C(=O)O)C(C)C`
ZINC1605719 ZINC	0.552	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@@H](C(=O)O)C(C)C`
ZINC1605720 ZINC	0.552	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@@H](C(=O)O)C(C)C`
ZINC249691100 ZINC	0.548	436.4 Da LogP 0.40 TPSA 169.3	1 viol.	Alert	`C[C@@H]1O[C@H](O[C@@H]2Cc3c(O)cc(O)cc3O[C@H]2c2…`
ZINC250898615 ZINC	0.548	436.4 Da LogP 0.40 TPSA 169.3	1 viol.	Alert	`C[C@H]1O[C@H](O[C@H]2Cc3c(O)cc(O)cc3O[C@H]2c2cc…`
ZINC38469525 ZINC	0.548	436.4 Da LogP 0.40 TPSA 169.3	1 viol.	Alert	`C[C@@H]1O[C@H](O[C@H]2Cc3c(O)cc(O)cc3O[C@@H]2c2…`

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.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

glutamate dehydrogenase

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways