Protein target profile

VK055_4299

amino-acid N-acetyltransferase

Genome: KpATCC43816 Gene: argA AIK82844.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GX20

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Length 442

Pocket druggability 0.919

Metabolic reactions 2

Chokepoint Yes

Direct ligand evidence 0 68 total records

Functional annotation 1 EC 5 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic bottleneck Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Review the complete evidence below

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: No hit
Gut microbiome similarity: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 51.724 Higher values support similarity to known essential genes.
DEG E-value: 5.48e-163 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 92.84 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.919

Structure A0A0H3GX20

Pocket Pocket 1

P2Rank 0.669

Structure A0A0H3GX20

Pocket Pocket 1

ColabFold model

FPocket 0.448 · Pocket 5

P2Rank 0.749 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 140 / 4744 genomes with a hit

Prevalence 3.0%

Cross-references

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

Sequence

UniProt A0A0H3GX20

Pathways

BioCyc RXN0-6948 KEGG R00259 BioCyc N-ACETYLTRANSFER-RXN

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Arginine biosynthesis, no isoenzyme backup detected, no human homolog detected.

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

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKERRTELVEGFRHSVPYINAHRGKTFVIMLGGEAIEHENFSNIVNDIGLLHSLGIRLVVVYGARPQIDTNLAEHHHEPVYHKQTRVTDAKTLELVKQAAGMLQLEITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEAIHRQLDSGAIVLMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVYNQAGEIVSELFPNEAQARVEELEADEDYNSGTVRFLRGAVKACRSGVRRCHLISYQENGALLQELFSRDGIGTQIVMESAEQIRRATINDIGGILELISPLEQQGILVRRSREQLEMEIDKFTIIQRDNTTIACAALYPFPEEKIGEMACVAVHPDYRSSSRGEVLLERIAAQARQMGLSKLFVLTTRSIHWFQERGFTPVDIDLLPESKKQMYNYQRRSKVLMADLA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

2.3.1.1

Gene Ontology (GO)

GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
GO:0006526 The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0004042 Catalysis of the reaction: L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H+.
GO:0004358 Catalysis of the reaction: N2-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate + L-ornithine.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
295	442	Gene3D	G3DSA:3.40.630.30	-
228	417	SUPERFAMILY	SSF55729	Acyl-CoA N-acyltransferases (Nat)
228	417	InterPro	IPR016181	Acyl-CoA N-acyltransferase
1	441	PIRSF	PIRSF000423	ArgA
1	441	InterPro	IPR010167	Amino-acid N-acetyltransferase
6	293	Gene3D	G3DSA:3.40.1160.10	-
6	293	InterPro	IPR036393	Acetylglutamate kinase-like superfamily
4	290	SUPERFAMILY	SSF53633	Carbamate kinase-like
4	290	InterPro	IPR036393	Acetylglutamate kinase-like superfamily
336	398	CDD	cd04301	NAT_SF
8	441	NCBIfam	TIGR01890	amino-acid N-acetyltransferase
8	441	InterPro	IPR010167	Amino-acid N-acetyltransferase
7	289	CDD	cd04237	AAK_NAGS-ABP
7	289	InterPro	IPR033719	N-acetylglutamate synthase, kinase-like domain
295	442	ProSiteProfiles	PS51186	Gcn5-related N-acetyltransferase (GNAT) domain profile.
295	442	InterPro	IPR000182	GNAT domain
1	441	Hamap	MF_01105	Amino-acid acetyltransferase [argA].
335	412	Pfam	PF00583	Acetyltransferase (GNAT) family
335	412	InterPro	IPR000182	GNAT domain
6	293	FunFam	G3DSA:3.40.1160.10:FF:000005	Amino-acid acetyltransferase
25	267	Pfam	PF00696	Amino acid kinase family
25	267	InterPro	IPR001048	Aspartate/glutamate/uridylate kinase
244	441	PANTHER	PTHR30602	AMINO-ACID ACETYLTRANSFERASE
244	441	InterPro	IPR010167	Amino-acid N-acetyltransferase
295	441	FunFam	G3DSA:3.40.630.30:FF:000009	Amino-acid acetyltransferase

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 · FPocket

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

Site 1 FPocket #1

0.919

Likely same site as P2Rank 1 2.5 Å 26 shared residues 100% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.669

Likely same site as FPocket 1 2.5 Å 26 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.489

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Surrounding area

Site 3 P2Rank #3

0.397

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Surrounding area

Site 4 P2Rank #4

0.066

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Surrounding area

Site 5 P2Rank #5

0.056

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #5

0.448

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Surrounding area

Site 2 FPocket #1

0.361

Likely same site as P2Rank 1 1.1 Å 30 shared residues 100% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.749

Likely same site as FPocket 1 1.1 Å 30 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.484

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Surrounding area

Site 3 P2Rank #3

0.374

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Surrounding area

Site 4 P2Rank #4

0.195

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Surrounding area

Site 5 P2Rank #5

0.07

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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_A0A0H3GX20	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4299	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.

68 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 18 records from similar proteins

Structural ligands 18 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

14N PDB via homolog 220.3 Da · LogP 1.14 · TPSA 43.8 Open detail RCSB PDB

5RN PDB via homolog Detail RCSB PDB

97Q PDB via homolog Detail RCSB PDB

97T PDB via homolog Detail RCSB PDB

97W 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
14N RCSB PDB	7NLT	P9WQ01	220.3 Da LogP 1.14 TPSA 43.8	✓ Ro5	✓ Clean	`CN1CCN(CC1)c2ccc(cc2)C(=O)O`
5RN RCSB PDB	7NLU	P9WQ01	159.2 Da LogP 2.37 TPSA 32.9	✓ Ro5	✓ Clean	`CC(=O)c1c[nH]c2c1cccc2`
97Q RCSB PDB	7NNB	P9WQ01	281.2 Da LogP 3.98 TPSA 33.1	✓ Ro5	✓ Clean	`c1cc2c(cc(nc2c(c1)C(F)(F)F)C(F)(F)F)O`
97T RCSB PDB	7NLQ	P9WQ01	161.2 Da LogP 2.05 TPSA 46.3	✓ Ro5	✓ Clean	`c1ccc(c(c1)c2ccno2)O`
97W RCSB PDB	7NLX	P9WQ01	213.2 Da LogP 2.96 TPSA 33.1	✓ Ro5	✓ Clean	`c1cc2c(ccnc2cc1C(F)(F)F)O`
98K RCSB PDB	7NLY	P9WQ01	152.6 Da LogP 2.22 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc2c(c1)[nH]c(n2)Cl`
98Q RCSB PDB	7NLZ	P9WQ01	215.2 Da LogP 3.20 TPSA 25.0	✓ Ro5	✓ Clean	`COc1cc2cc[nH]c2cc1C(F)(F)F`
98T RCSB PDB	7NLS	P9WQ01	278.0 Da LogP 1.78 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(c(c1)I)O`
98W RCSB PDB	7NN7	P9WQ01	210.2 Da LogP 0.97 TPSA 72.8	✓ Ro5	✓ Clean	`COC(=O)c1cc(cc(c1)O)C(=O)OC`
98Z RCSB PDB	7NN8	P9WQ01	142.2 Da LogP 2.04 TPSA 39.6	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)C#N`
9EQ RCSB PDB	7NM0	P9WQ01	152.1 Da LogP 1.30 TPSA 57.5	✓ Ro5	✓ Clean	`CC(=O)c1c(cccc1O)O`
GGB RCSB PDB	7NLP	P9WQ01	176.2 Da LogP -1.80 TPSA 134.5	✓ Ro5	✓ Clean	`[H]/N=C(\N)/NOCC[C@@H](C(=O)O)N`
MLI RCSB PDB	3ZZH	Q01217	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
NHE RCSB PDB	7NLO	P9WQ01	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=O)(=O)O`
NLG RCSB PDB	2JJ4	Q6V1L5	189.2 Da LogP -0.56 TPSA 103.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCC(=O)O)C(=O)O`
PIY RCSB PDB	7NLR	P9WQ01	144.2 Da LogP 2.08 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc(cc1)c2[nH]ccn2`
UOK RCSB PDB	7NLW	P9WQ01	186.2 Da LogP 2.24 TPSA 48.8	✓ Ro5	✓ Clean	`COc1ccc2c(c1)c(c[nH]2)CC#N`
X2W RCSB PDB	4USJ	Q9SCL7	269.1 Da LogP -1.01 TPSA 150.2	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCC(=O)OP(=O)(O)O)C(=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).

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
ZINC158905 ZINC	1.000	220.3 Da LogP 1.14 TPSA 43.8	✓ Ro5	✓ Clean	`CN1CCN(c2ccc(C(=O)O)cc2)CC1`
ZINC1710230 ZINC	1.000	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC2548331 ZINC	1.000	278.0 Da LogP 1.78 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(O)c(I)c1`
ZINC32327 ZINC	1.000	210.2 Da LogP 0.97 TPSA 72.8	✓ Ro5	✓ Clean	`COC(=O)c1cc(O)cc(C(=O)OC)c1`
ZINC34503706 ZINC	1.000	215.2 Da LogP 3.20 TPSA 25.0	✓ Ro5	✓ Clean	`COc1cc2cc[nH]c2cc1C(F)(F)F`
ZINC8830538 ZINC	1.000	281.2 Da LogP 3.98 TPSA 33.1	✓ Ro5	✓ Clean	`Oc1cc(C(F)(F)F)nc2c(C(F)(F)F)cccc12`
ZINC89202735 ZINC	0.913	220.3 Da LogP 3.74 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc(-c2ccc(-c3ncc[nH]3)cc2)cc1`
ZINC12370640 ZINC	0.862	234.3 Da LogP 1.53 TPSA 43.8	✓ Ro5	✓ Clean	`CN1CCCN(c2ccc(C(=O)O)cc2)CC1`
ZINC1532510 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=…`
ZINC1532511 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O…`
ZINC1532512 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](CCC(=O)O)C(=O…`
ZINC1532513 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)O)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC56412 ZINC	0.800	252.2 Da LogP 1.05 TPSA 78.9	✓ Ro5	✓ Clean	`COC(=O)c1cc(C(=O)OC)cc(C(=O)OC)c1`
ZINC2504638 ZINC	0.793	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=…`
ZINC4534089 ZINC	0.793	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O…`
ZINC4534090 ZINC	0.793	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O…`
ZINC4534091 ZINC	0.793	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC2004372 ZINC	0.786	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153 ZINC	0.786	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC169847 ZINC	0.759	218.3 Da LogP 1.64 TPSA 23.6	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N2CCN(C)CC2)cc1`
ZINC15923743 ZINC	0.743	227.2 Da LogP 3.27 TPSA 33.1	✓ Ro5	✓ Clean	`Cc1cccc2c(O)cc(C(F)(F)F)nc12`
ZINC2560824 ZINC	0.733	260.2 Da LogP -1.05 TPSA 132.8	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC82264502 ZINC	0.733	219.3 Da LogP 0.54 TPSA 49.6	✓ Ro5	✓ Clean	`CN1CCN(c2ccc(C(N)=O)cc2)CC1`
ZINC8700304 ZINC	0.733	278.0 Da LogP 1.78 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(I)c(O)c1`
ZINC51951733 ZINC	0.731	278.0 Da LogP 1.78 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1cc(O)cc(I)c1`
ZINC58123315 ZINC	0.731	376.3 Da LogP -1.36 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CCC(=O)N[C@@H](CCC(=O)O)C(=…`
ZINC58123320 ZINC	0.731	376.3 Da LogP -1.36 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CCC(=O)N[C@H](CCC(=O)O)C(=O…`
ZINC58123326 ZINC	0.731	376.3 Da LogP -1.36 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@@H](NC(=O)CCC(=O)N[C@H](CCC(=O)O)C(=…`
ZINC65336911 ZINC	0.731	231.0 Da LogP 1.94 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1cc(O)cc(Br)c1`
ZINC71789975 ZINC	0.727	215.0 Da LogP 2.36 TPSA 37.3	✓ Ro5	✓ Clean	`CC(=O)c1c(O)cccc1Br`
ZINC156144 ZINC	0.714	231.1 Da LogP 3.10 TPSA 33.1	✓ Ro5	✓ Clean	`Oc1cc(C(F)(F)F)nc2c(F)cccc12`
ZINC20079899 ZINC	0.714	282.3 Da LogP 2.71 TPSA 43.8	✓ Ro5	✓ Clean	`O=C(O)c1ccc(N2CCN(c3ccccc3)CC2)cc1`
ZINC163194744 ZINC	0.707	214.3 Da LogP 3.02 TPSA 48.8	✓ Ro5	✓ Clean	`CCCOc1ccc2[nH]cc(CC#N)c2c1`
ZINC1530296 ZINC	0.704	247.2 Da LogP -0.71 TPSA 141.0	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC44185391 ZINC	0.704	208.3 Da LogP 2.48 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1cc(O)cc(C(C)(C)C)c1`
ZINC2457232 ZINC	0.700	248.3 Da LogP 1.05 TPSA 60.9	✓ Ro5	✓ Clean	`CC(=O)N1CCN(c2ccc(C(=O)O)cc2)CC1`
ZINC97437871 ZINC	0.696	262.0 Da LogP 2.20 TPSA 37.3	✓ Ro5	✓ Clean	`CC(=O)c1c(O)cccc1I`
ZINC135889580 ZINC	0.694	295.2 Da LogP 3.76 TPSA 33.1	✓ Ro5	✓ Clean	`OCc1cc(C(F)(F)F)nc2c(C(F)(F)F)cccc12`
ZINC157271 ZINC	0.694	247.6 Da LogP 3.61 TPSA 33.1	✓ Ro5	✓ Clean	`Oc1cc(C(F)(F)F)nc2c(Cl)cccc12`
ZINC161361 ZINC	0.694	292.1 Da LogP 3.72 TPSA 33.1	✓ Ro5	✓ Clean	`Oc1cc(C(F)(F)F)nc2c(Br)cccc12`
ZINC34620790 ZINC	0.694	339.1 Da LogP 3.56 TPSA 33.1	✓ Ro5	✓ Clean	`Oc1cc(C(F)(F)F)nc2c(I)cccc12`
ZINC13529664 ZINC	0.692	320.3 Da LogP -1.08 TPSA 190.3	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=…`
ZINC2572074 ZINC	0.690	203.2 Da LogP -0.47 TPSA 92.7	✓ Ro5	✓ Clean	`COC(=O)[C@H](CCC(=O)O)NC(C)=O`
ZINC56960616 ZINC	0.690	203.2 Da LogP -0.47 TPSA 92.7	✓ Ro5	✓ Clean	`COC(=O)[C@@H](CCC(=O)O)NC(C)=O`
ZINC1384102 ZINC	0.688	234.3 Da LogP 1.22 TPSA 32.8	✓ Ro5	✓ Clean	`COC(=O)c1ccc(N2CCN(C)CC2)cc1`
ZINC2540734 ZINC	0.688	263.3 Da LogP 0.56 TPSA 103.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CS[C@H](C)CCC(=O)O)C(=O)O`
ZINC32089653 ZINC	0.688	232.3 Da LogP 2.03 TPSA 23.6	✓ Ro5	✓ Clean	`CCC(=O)c1ccc(N2CCN(C)CC2)cc1`
ZINC83263397 ZINC	0.688	263.3 Da LogP 0.56 TPSA 103.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CS[C@@H](C)CCC(=O)O)C(=O)O`
ZINC2149531 ZINC	0.686	299.6 Da LogP 4.93 TPSA 12.9	✓ Ro5	✓ Clean	`FC(F)(F)c1cc(Cl)c2cccc(C(F)(F)F)c2n1`
ZINC32099772 ZINC	0.686	279.2 Da LogP 4.58 TPSA 12.9	✓ Ro5	✓ Clean	`Cc1cc(C(F)(F)F)nc2c(C(F)(F)F)cccc12`

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.