Genome KpKP13

Protein target profile

Anaerobic glycerol-3-phosphate dehydrogenase subunit A

Accession: KP13_00962

Gene: AHE43508.1 glpA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GW84

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Length 540

Pocket druggability (P2Rank · AlphaFold DB model) 0.975

Direct ligand evidence 0 51 total records

Functional annotation 1 EC 10 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

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

Main supporting evidence

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.97, FPocket 0.82). Use the 3D pocket comparison to verify whether they identify the same site. Strong predicted binding pocket FPocket selected-pocket score 0.82. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.97. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

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 (%): 50.0 Lower values reduce human off-target concern.
Human E-value: 5.53e-06
Gut microbiome similarity: 5.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 68.431 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 93.3 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) 0.975

Structure A0A0H3GW84

Pocket Pocket 1

Druggability (FPocket) 0.822

Structure A0A0H3GW84

Pocket Pocket 5

ColabFold model

P2Rank 0.982 · Pocket 1

FPocket 0.677 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 253 / 4744 genomes with a hit

Prevalence 5.3%

Cross-references

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

Sequence

UniProt A0A0H3GW84

Sequence

Primary amino-acid sequence viewer.

MTGRLDSEVIIIGGGATGAGIARDCARRGLRTLLIERHDIATGATGRNHGLLHSGARYAVTDNESARECISENRILRRIARHCIEPTNGLFITLPEDDLAWQQTFIDACQQAGIEATPLSPQEALRREPAVNPTLLGAVQVPDGTIDPFRLTAANMLDAREHGAQILTGCEVTGLLRRGDRVCGVQVYDRQLHQARTLYAGMVVNAAGIWGQRIAEYADLRITMFPAKGSLLILDHRINNLVINRCRKPADADILVPGDTISLIGTTSMHIPYDEIDDNRVTAAEVDTLLREGEKLAPVMGRTRILRAYSGVRPLVASDNDPSGRSVSRGIVLLDHAQRDGMEGFITITGGKLMTYRLMAEWATDAVCRKLGNTTPCTTAEAPLPGSQEPTESTLQKIISLPTPLRGSAVYRHGDRTPSWLGDSRQHRSLVCECEAVTAGEVKYAVENLAVNTLLDLRRRTRIGMGTCQGELCACRAAGLLQRFNVTTPAQSLTQLSEFLNERWKGVQPIAWGDALRESEFTRWVYLGLCGLPQEHRDEV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.1.5.3

Gene Ontology (GO)

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:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0009331 An enzyme complex that catalyzes the oxidation of sn-glycerol 3-phosphate to dihydroxyacetone phosphate, with concurrent reduction of flavin adenine dinucleotide (FAD) to FADH2. In E. coli, the complex is either a GlpA-GlpB-GlpC heterotrimer that functions in anaerobic conditions, or a GlpD homodimer that functions in aerobic conditions.
GO:0006072 The chemical reactions and pathways involving glycerol-3-phosphate, a phosphoric monoester of glycerol.
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:0004368 Catalysis of the reaction: sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
GO:0046174 The chemical reactions and pathways resulting in the breakdown of a polyol, any alcohol containing three or more hydroxyl groups attached to saturated carbon atoms.
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0019563 The chemical reactions and pathways resulting in the breakdown of glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
GO:0046168 The chemical reactions and pathways resulting in the breakdown of glycerol-3-phosphate, a phosphoric monoester of glycerol.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
418	491	Gene3D	G3DSA:1.10.10.1100	-
418	491	InterPro	IPR041854	BFD-like [2Fe-2S]-binding domain superfamily
12	29	ProSitePatterns	PS00977	FAD-dependent glycerol-3-phosphate dehydrogenase signature 1.
12	29	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
312	392	FunFam	G3DSA:3.50.50.60:FF:000096	Glycerol-3-phosphate dehydrogenase
8	536	NCBIfam	TIGR03377	anaerobic glycerol-3-phosphate dehydrogenase subunit GlpA
8	536	InterPro	IPR017752	Glycerol-3-phosphate dehydrogenase, GlpA subunit
8	525	PANTHER	PTHR11985	GLYCEROL-3-PHOSPHATE DEHYDROGENASE
8	525	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
2	120	FunFam	G3DSA:3.50.50.60:FF:000102	Glycerol-3-phosphate dehydrogenase
9	357	Pfam	PF01266	FAD dependent oxidoreductase
9	357	InterPro	IPR006076	FAD dependent oxidoreductase
3	117	Gene3D	G3DSA:3.50.50.60	-
3	117	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
122	248	Gene3D	G3DSA:3.50.50.60	-
122	248	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
418	490	FunFam	G3DSA:1.10.10.1100:FF:000003	Glycerol-3-phosphate dehydrogenase
298	388	Gene3D	G3DSA:3.50.50.60	-
298	388	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
80	92	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
80	92	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
20	30	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
20	30	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
36	48	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
36	48	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
345	357	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
345	357	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
7	19	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
7	19	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
309	315	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
309	315	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
350	360	ProSitePatterns	PS00978	FAD-dependent glycerol-3-phosphate dehydrogenase signature 2.
430	483	CDD	cd19946	GlpA-like_Fer2_BFD-like
224	315	SUPERFAMILY	SSF54373	FAD-linked reductases, C-terminal domain
430	482	Pfam	PF04324	BFD-like [2Fe-2S] binding domain
430	482	InterPro	IPR007419	BFD-like [2Fe-2S]-binding domain
8	320	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
8	320	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily

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

0.975

Likely same site as FPocket 1 1.9 Å 50 shared residues 94% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.905

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Surrounding area

Pocket 3 P2Rank #3

0.11

Likely same site as FPocket 5 0.9 Å 13 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.05

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Surrounding area

Pocket 5 P2Rank #5

0.034

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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 #5

0.822 Unusual size

Likely same site as P2Rank 3 0.9 Å 13 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #1

0.36 Unusual size

Likely same site as P2Rank 1 1.9 Å 50 shared residues 94% of smaller site

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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

0.982

Likely same site as FPocket 1 5.9 Å 46 shared residues 98% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.873

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Surrounding area

Pocket 3 P2Rank #3

0.025

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Surrounding area

Pocket 4 P2Rank #4

0.01

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Surrounding area

Pocket 5 P2Rank #5

0.002

Likely same site as FPocket 1 6.1 Å 5 shared residues 71% 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_A0A0H3GW84	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00962	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.

51 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 1 records from similar proteins

Structural ligands 1 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

THG PDB via homolog 445.4 Da · LogP -0.28 · TPSA 211.6 Open detail RCSB PDB

ZINC4228235 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC4228236 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC4228237 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC4228238 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

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
THG RCSB PDB	4PAA	Q63342	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@H]2C…`

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
ZINC4228235 ZINC	1.000	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CNc1ccc(C(=O)N[C@@H](…`
ZINC4228236 ZINC	1.000	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CNc1ccc(C(=O)N[C@H](C…`
ZINC4228237 ZINC	1.000	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H](CNc1ccc(C(=O)N[C@@H]…`
ZINC4228238 ZINC	1.000	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H](CNc1ccc(C(=O)N[C@H](…`
ZINC8618631 ZINC	0.848	459.5 Da LogP 0.11 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CCNc1ccc(C(=O)N[C@@H]…`
ZINC8627114 ZINC	0.848	459.5 Da LogP 0.11 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H](CCNc1ccc(C(=O)N[C@@H…`
ZINC4228247 ZINC	0.712	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CN(C=O)c1ccc(C(=O)N[C…`
ZINC2005305 ZINC	0.708	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@@H]1CNc1ccc(C(=O)N[C@…`
ZINC2572666 ZINC	0.708	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@H]1CNc1ccc(C(=O)N[C@@…`
ZINC4228266 ZINC	0.708	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@@H]1CNc1ccc(C(=O)N[C@…`
ZINC4228267 ZINC	0.708	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@H]1CNc1ccc(C(=O)N[C@H…`
ZINC9212425 ZINC	0.689	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CNc1ccc(C(=O)N[…`
ZINC9212426 ZINC	0.689	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@H](CNc1ccc(C(=O)N[C…`
ZINC9212427 ZINC	0.689	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CNc1ccc(C(=O)N[…`
ZINC9212428 ZINC	0.689	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@H](CNc1ccc(C(=O)N[C…`
ZINC8618632 ZINC	0.635	459.5 Da LogP 0.52 TPSA 211.8	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@@H](CCNc1ccc(C(=O)N[C@H](CC…`
ZINC8627115 ZINC	0.635	459.5 Da LogP 0.52 TPSA 211.8	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@H](CCNc1ccc(C(=O)N[C@H](CCC…`
ZINC4228265 ZINC	0.630	443.4 Da LogP 0.01 TPSA 211.9	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N=C(CNc1ccc(C(=O)N[C@@H](CCC…`
ZINC4517559 ZINC	0.630	443.4 Da LogP 0.01 TPSA 211.9	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N=C(CNc1ccc(C(=O)N[C@H](CCC(…`
ZINC8655682 ZINC	0.628	487.5 Da LogP -0.34 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CCNc1ccc(C(=O)N…`
ZINC13887836 ZINC	0.616	429.4 Da LogP 0.54 TPSA 187.5	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)[C@@H](CCc1ccc(C(=O)N[C@@H](…`
ZINC4658141 ZINC	0.608	443.5 Da LogP 0.62 TPSA 187.5	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)C[C@H](CCc1ccc(C(=O)N[C@H](C…`
ZINC4658144 ZINC	0.608	443.5 Da LogP 0.62 TPSA 187.5	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)C[C@@H](CCc1ccc(C(=O)N[C@H](…`
ZINC4228269 ZINC	0.605	456.4 Da LogP -0.61 TPSA 193.7	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)[N+]1=CN(c3ccc(C(=O)N[C@@H](…`
ZINC4228270 ZINC	0.605	456.4 Da LogP -0.61 TPSA 193.7	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)[N+]1=CN(c3ccc(C(=O)N[C@@H](…`
ZINC4654270 ZINC	0.592	471.4 Da LogP -0.36 TPSA 211.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1C(=O)N(c3ccc(C(=O)N[C@@H](…`
ZINC4654271 ZINC	0.592	471.4 Da LogP -0.36 TPSA 211.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1C(=O)N(c3ccc(C(=O)N[C@@H](…`
ZINC13515262 ZINC	0.589	439.4 Da LogP 1.17 TPSA 187.5	1 viol.	✓ Clean	`Nc1nc2ccc(CNc3ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)…`
ZINC4228243 ZINC	0.584	457.4 Da LogP -0.52 TPSA 194.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1CN(c3ccc(C(=O)N[C@@H](CCC(…`
ZINC4228244 ZINC	0.584	457.4 Da LogP -0.52 TPSA 194.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1CN(c3ccc(C(=O)N[C@H](CCC(=…`
ZINC4654260 ZINC	0.584	457.4 Da LogP -0.52 TPSA 194.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1CN(c3ccc(C(=O)N[C@@H](CCC(…`
ZINC8664075 ZINC	0.580	330.3 Da LogP 0.76 TPSA 145.2	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H](CCNc1ccc(C(=O)O)cc1)…`
ZINC77301924 ZINC	0.573	443.4 Da LogP 0.07 TPSA 204.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)[C@H](CCc1ccc(C(=O)N[C@H](CC…`
ZINC1567048 ZINC	0.568	440.4 Da LogP 0.56 TPSA 200.4	1 viol.	✓ Clean	`Nc1nc2ccc(CNc3ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)…`
ZINC1995991 ZINC	0.568	439.4 Da LogP 1.17 TPSA 187.5	1 viol.	✓ Clean	`Nc1nc2ccc(NCc3ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)…`
ZINC4261891 ZINC	0.560	441.4 Da LogP -0.04 TPSA 213.3	1 viol.	✓ Clean	`Nc1nc2nc(CNc3ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)c…`
ZINC17380277 ZINC	0.551	469.5 Da LogP 0.39 TPSA 213.3	1 viol.	✓ Clean	`Nc1nc2ncc(CCCNc3ccc(C(=O)N[C@H](CCC(=O)O)C(=O)O…`
ZINC31350053 ZINC	0.551	458.5 Da LogP 0.03 TPSA 208.8	1 viol.	✓ Clean	`CN(C[C@@H]1CNc2nc(N)nc(N)c2N1)c1ccc(C(=O)N[C@@H…`
ZINC31350056 ZINC	0.551	458.5 Da LogP 0.03 TPSA 208.8	1 viol.	✓ Clean	`CN(C[C@H]1CNc2nc(N)nc(N)c2N1)c1ccc(C(=O)N[C@@H]…`
ZINC4826295 ZINC	0.551	469.5 Da LogP 0.39 TPSA 213.3	1 viol.	✓ Clean	`Nc1nc2ncc(CCCNc3ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)…`
ZINC8536462 ZINC	0.550	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC[C@H](CN(C=O)c1ccc(C(=O)N[…`
ZINC8628600 ZINC	0.550	473.5 Da LogP 0.13 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c([nH]c(N)nc2=O)NC[C@@H]1CCNc1ccc(C(=O)N[C…`
ZINC8628601 ZINC	0.550	473.5 Da LogP 0.13 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c([nH]c(N)nc2=O)NC[C@H]1CCNc1ccc(C(=O)N[C@…`
ZINC8642279 ZINC	0.548	432.4 Da LogP 0.03 TPSA 213.5	1 viol.	✓ Clean	`Nc1nc(=O)c(CCCNc2ccc(C(=O)N[C@@H](CCC(=O)O)C(=O…`
ZINC5385736 ZINC	0.547	439.4 Da LogP 1.17 TPSA 187.5	1 viol.	✓ Clean	`Nc1nc(=O)c2cc(NCc3ccc(C(=O)N[C@H](CCC(=O)O)C(=O…`
ZINC1689613 ZINC	0.539	442.5 Da LogP 0.91 TPSA 193.5	1 viol.	✓ Clean	`Nc1nc(N)c2c(n1)CC[C@H](CNc1ccc(C(=O)N[C@@H](CCC…`
ZINC1689614 ZINC	0.539	442.5 Da LogP 0.91 TPSA 193.5	1 viol.	✓ Clean	`Nc1nc(N)c2c(n1)CC[C@@H](CNc1ccc(C(=O)N[C@@H](CC…`
ZINC1689615 ZINC	0.539	442.5 Da LogP 0.91 TPSA 193.5	1 viol.	✓ Clean	`Nc1nc(N)c2c(n1)CC[C@H](CNc1ccc(C(=O)N[C@H](CCC(…`
ZINC1689616 ZINC	0.539	442.5 Da LogP 0.91 TPSA 193.5	1 viol.	✓ Clean	`Nc1nc(N)c2c(n1)CC[C@@H](CNc1ccc(C(=O)N[C@H](CCC…`
ZINC1605633 ZINC	0.538	444.5 Da LogP -1.44 TPSA 216.5	1 viol.	✓ Clean	`NC1=NC(N)=C2N[C@@H](CNc3ccc(C(=O)N[C@@H](CCC(=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.