Protein target profile

KP13_04673

phenylalanyl-tRNA synthetase alpha subunit

Genome: KpKP13 Gene: pheS AHE44067.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GU78

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Length 331

Pocket druggability 0.595

Direct ligand evidence 0 59 total records

Functional annotation 1 EC 9 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.59. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.93. 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 (%): 33.333 Lower values reduce human off-target concern.
Human E-value: 3.03e-10
Gut microbiome similarity: 20.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 96.979 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 93.98 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 0.595

Structure A0A0H3GU78

Pocket Pocket 1

P2Rank 0.933

Structure A0A0H3GU78

Pocket Pocket 1

ColabFold model

FPocket 0.591 · Pocket 7

P2Rank 0.871 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 975 / 4744 genomes with a hit

Prevalence 20.6%

Cross-references

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

Sequence

UniProt A0A0H3GU78

Chemistry

ChEMBL CHEMBL197403

Sequence

Primary amino-acid sequence viewer.

MRKTMSHLAELVASAKAAINEASDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELEGAALNARLAAETIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDATRLLRTQTSGVQIRTMENQQPPIRIIAPGRVYRNDYDQTHTPMFHQMEGLIVDKNISFTNLKGTLHDFLNNFFEEDLQVRFRPSYFPFTEPSAEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYGVTDLRAFFENDLRFLKQFK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

6.1.1.20

Gene Ontology (GO)

GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0004826 Catalysis of the reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
GO:0000049 Binding to a transfer RNA.
GO:0006432 The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0043039 The chemical reactions and pathways by which the various amino acids become bonded to their corresponding tRNAs. The most common route for synthesis of aminoacyl tRNA is by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules.
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:0000287 Binding to a magnesium (Mg) ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
12	331	FunFam	G3DSA:3.30.930.10:FF:000003	Phenylalanine--tRNA ligase alpha subunit
111	325	CDD	cd00496	PheRS_alpha_core
18	103	SUPERFAMILY	SSF46589	tRNA-binding arm
18	103	InterPro	IPR010978	Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm
96	330	Pfam	PF01409	tRNA synthetases class II core domain (F)
96	330	InterPro	IPR002319	Phenylalanyl-tRNA synthetase
42	331	NCBIfam	TIGR00468	phenylalanine--tRNA ligase subunit alpha
42	331	InterPro	IPR004529	Phenylalanyl-tRNA synthetase, class IIc, alpha subunit
96	331	SUPERFAMILY	SSF55681	Class II aaRS and biotin synthetases
96	331	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
65	85	Coils	Coil	Coil
12	331	Gene3D	G3DSA:3.30.930.10	Bira Bifunctional Protein; Domain 2
12	331	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
120	321	ProSiteProfiles	PS50862	Aminoacyl-transfer RNA synthetases class-II family profile.
120	321	InterPro	IPR006195	Aminoacyl-tRNA synthetase, class II
24	91	Pfam	PF02912	Aminoacyl tRNA synthetase class II, N-terminal domain
24	91	InterPro	IPR004188	Phenylalanine-tRNA ligase, class II, N-terminal
12	330	Hamap	MF_00281	Phenylalanine--tRNA ligase alpha subunit [pheS].
12	330	InterPro	IPR022911	Phenylalanine-tRNA ligase alpha chain 1, bacterial
327	331	Coils	Coil	Coil
97	331	PANTHER	PTHR11538	PHENYLALANYL-TRNA SYNTHETASE

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

0.595

Likely same site as P2Rank 1 0.7 Å 34 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

0.933

Likely same site as FPocket 1 0.7 Å 34 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.251

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Surrounding area

Site 3 P2Rank #3

0.052

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Surrounding area

Site 4 P2Rank #4

0.037

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Surrounding area

Site 5 P2Rank #5

0.032

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Surrounding area

Residue sets

UniProt: Binding site:252-252

Binding pockets · FPocket

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

Site 1 FPocket #7

0.591

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Surrounding area

Site 2 FPocket #4

0.257

Likely same site as P2Rank 1 2.9 Å 26 shared residues 93% of smaller site

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.871

Likely same site as FPocket 4 2.9 Å 26 shared residues 93% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.23

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Surrounding area

Site 3 P2Rank #3

0.154

Likely same site as FPocket 4 5.7 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.081

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Surrounding area

Site 5 P2Rank #5

0.059

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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_A0A0H3GU78	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04673	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.

59 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2NL PDB via homolog 291.7 Da · LogP 2.60 · TPSA 63.2 Open detail RCSB PDB

2NM PDB via homolog Detail RCSB PDB

2U9 PDB via homolog Detail RCSB PDB

GAX PDB via homolog Detail RCSB PDB

H2L 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
2NL RCSB PDB	4P72	Q9I0A3	291.7 Da LogP 2.60 TPSA 63.2	✓ Ro5	✓ Clean	`CNC(=O)COc1cccc(c1)Nc2cc(ccn2)Cl`
2NM RCSB PDB	4P75	Q9I0A3	242.2 Da LogP 3.10 TPSA 37.9	✓ Ro5	✓ Clean	`COc1cccc(c1)c2cc([nH]n2)C(F)(F)F`
2U9 RCSB PDB	4P74	Q9I0A3	366.5 Da LogP 1.95 TPSA 85.4	✓ Ro5	✓ Clean	`Cc1ccc(cc1)OCc2nc(cs2)C(=O)N[C@H]3CCS(=O)(=O)C3`
GAX RCSB PDB	2RHQ	Q4L5E3	444.5 Da LogP 2.69 TPSA 107.5	✓ Ro5	✓ Clean	`c1ccnc(c1)N2CCN(CC2)S(=O)(=O)c3cccc(c3)NC(=O)Nc…`
H2L RCSB PDB	7DB7	P9WFU3	441.5 Da LogP 3.79 TPSA 116.0	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)CCNS(=O)(=O)c3cccc(c3)NC(=O…`
H2R RCSB PDB	7DB8	P9WFU3	456.5 Da LogP 5.77 TPSA 67.3	1 viol.	✓ Clean	`c1cc(cc(c1)Oc2ccc(cn2)C(F)(F)F)CC3CCN(CC3)C(=O)…`
NO4 RCSB PDB	6P26	P08312	215.3 Da LogP 3.67 TPSA 12.0	✓ Ro5	✓ Clean	`c1ccc(cc1)CNCCC2=CCCCC2`
VB3 RCSB PDB	6OZ5	P08312	247.4 Da LogP 3.84 TPSA 32.3	✓ Ro5	Alert	`C[C@@H](CC1CCCCC1)NCc2ccccc2O`

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
CHEMBL197403 ChEMBL	P68849	6.80 ~158.5 nM	295.3 Da LogP 3.53 TPSA 32.3	✓ Ro5	✓ Clean	`OC(CNCc1ccccc1)c1cccc(C(F)(F)F)c1`

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
ZINC2132373 ZINC	1.000	215.3 Da LogP 3.67 TPSA 12.0	✓ Ro5	✓ Clean	`C1=C(CCNCc2ccccc2)CCCC1`
ZINC34875345 ZINC	1.000	247.4 Da LogP 3.84 TPSA 32.3	✓ Ro5	Alert	`C[C@@H](CC1CCCCC1)NCc1ccccc1O`
ZINC45166848 ZINC	1.000	247.4 Da LogP 3.84 TPSA 32.3	✓ Ro5	Alert	`C[C@H](CC1CCCCC1)NCc1ccccc1O`
ZINC8734309 ZINC	1.000	366.5 Da LogP 1.95 TPSA 85.4	✓ Ro5	✓ Clean	`Cc1ccc(OCc2nc(C(=O)N[C@@H]3CCS(=O)(=O)C3)cs2)cc1`
ZINC8734310 ZINC	1.000	366.5 Da LogP 1.95 TPSA 85.4	✓ Ro5	✓ Clean	`Cc1ccc(OCc2nc(C(=O)N[C@H]3CCS(=O)(=O)C3)cs2)cc1`
ZINC408525452 ZINC	0.969	229.4 Da LogP 4.06 TPSA 12.0	✓ Ro5	✓ Clean	`C1=C(CCNCc2ccccc2)CCCCC1`
ZINC120168678 ZINC	0.906	201.3 Da LogP 3.28 TPSA 12.0	✓ Ro5	✓ Clean	`C1=C(CCNCc2ccccc2)CCC1`
ZINC12877192 ZINC	0.821	386.9 Da LogP 2.29 TPSA 85.4	✓ Ro5	✓ Clean	`O=C(N[C@@H]1CCS(=O)(=O)C1)c1csc(COc2ccc(Cl)cc2)…`
ZINC12877196 ZINC	0.821	386.9 Da LogP 2.29 TPSA 85.4	✓ Ro5	✓ Clean	`O=C(N[C@H]1CCS(=O)(=O)C1)c1csc(COc2ccc(Cl)cc2)n1`
ZINC13718398 ZINC	0.794	229.4 Da LogP 3.71 TPSA 12.0	✓ Ro5	✓ Clean	`C1=C(CCNCCc2ccccc2)CCCC1`
ZINC113264413 ZINC	0.778	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC113264415 ZINC	0.778	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC2244337 ZINC	0.778	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2244338 ZINC	0.778	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC1834294 ZINC	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(C[C@H](N)C(=O)O)c1)C(=O)O`
ZINC1834295 ZINC	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O`
ZINC1834297 ZINC	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O`
ZINC14244804 ZINC	0.759	316.4 Da LogP 3.70 TPSA 51.2	✓ Ro5	✓ Clean	`Cc1ccc(OCc2nc(C(=O)NC3CCCC3)cs2)cc1`
ZINC2132374 ZINC	0.750	229.4 Da LogP 3.98 TPSA 12.0	✓ Ro5	✓ Clean	`Cc1ccc(CNCCC2=CCCCC2)cc1`
ZINC2132378 ZINC	0.750	233.3 Da LogP 3.81 TPSA 12.0	✓ Ro5	✓ Clean	`Fc1ccc(CNCCC2=CCCCC2)cc1`
ZINC2132380 ZINC	0.750	249.8 Da LogP 4.32 TPSA 12.0	✓ Ro5	✓ Clean	`Clc1ccc(CNCCC2=CCCCC2)cc1`
ZINC87493315 ZINC	0.746	412.5 Da LogP 4.74 TPSA 67.3	✓ Ro5	✓ Clean	`C#Cc1ccc(Oc2cccc(CC3CCN(C(=O)Nc4cccnc4)CC3)c2)n…`
ZINC12818736 ZINC	0.745	330.5 Da LogP 4.09 TPSA 51.2	✓ Ro5	✓ Clean	`Cc1ccc(OCc2nc(C(=O)NC3CCCCC3)cs2)cc1`
ZINC38350773 ZINC	0.735	201.3 Da LogP 3.28 TPSA 12.0	✓ Ro5	✓ Clean	`C1=C(CNCc2ccccc2)CCCC1`
ZINC39351856 ZINC	0.731	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
ZINC13717847 ZINC	0.730	216.3 Da LogP 3.06 TPSA 24.9	✓ Ro5	✓ Clean	`C1=C(CCNCc2ccncc2)CCCC1`
ZINC35111609 ZINC	0.725	295.3 Da LogP 3.53 TPSA 32.3	✓ Ro5	✓ Clean	`O[C@H](CNCc1ccc(C(F)(F)F)cc1)c1ccccc1`
ZINC35111611 ZINC	0.725	295.3 Da LogP 3.53 TPSA 32.3	✓ Ro5	✓ Clean	`O[C@@H](CNCc1ccc(C(F)(F)F)cc1)c1ccccc1`
ZINC2561081 ZINC	0.724	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC2561082 ZINC	0.724	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC13718511 ZINC	0.718	259.3 Da LogP 3.36 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccc(CNCCC2=CCCCC2)cc1`
ZINC4699522 ZINC	0.718	229.4 Da LogP 3.98 TPSA 12.0	✓ Ro5	✓ Clean	`Cc1cccc(CNCCC2=CCCCC2)c1`
ZINC8972933 ZINC	0.703	242.2 Da LogP 3.10 TPSA 37.9	✓ Ro5	✓ Clean	`COc1ccc(-c2cc(C(F)(F)F)[nH]n2)cc1`
ZINC113539705 ZINC	0.700	265.3 Da LogP 2.04 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C#Cc2ccccc2)cc1)C(=O)O`
ZINC113539708 ZINC	0.700	265.3 Da LogP 2.04 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C#Cc2ccccc2)cc1)C(=O)O`
ZINC116910786 ZINC	0.700	269.3 Da LogP 3.06 TPSA 88.0	✓ Ro5	Alert	`N[C@@H](Cc1ccc(/N=N/c2ccccc2)cc1)C(=O)O`
ZINC13717854 ZINC	0.700	216.3 Da LogP 3.06 TPSA 24.9	✓ Ro5	✓ Clean	`C1=C(CCNCc2cccnc2)CCCC1`
ZINC29566843 ZINC	0.700	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1cccc(-c2ccccc2)c1)C(=O)O`
ZINC29570997 ZINC	0.700	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(-c2ccccc2)c1)C(=O)O`
ZINC34843477 ZINC	0.700	245.3 Da LogP 2.65 TPSA 32.3	✓ Ro5	✓ Clean	`O[C@H](CNCc1ccccc1)c1cccc(F)c1`
ZINC37873784 ZINC	0.700	245.3 Da LogP 2.65 TPSA 32.3	✓ Ro5	✓ Clean	`O[C@@H](CNCc1ccccc1)c1cccc(F)c1`
ZINC44283581 ZINC	0.700	257.3 Da LogP 2.43 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccccc2)cc1)C(=O)O`
ZINC44283583 ZINC	0.700	257.3 Da LogP 2.43 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccccc2)cc1)C(=O)O`
ZINC13718338 ZINC	0.692	258.4 Da LogP 3.73 TPSA 15.3	✓ Ro5	Alert	`CN(C)c1ccc(CNCCC2=CCCCC2)cc1`
ZINC2111574 ZINC	0.692	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1C[C@H](N)C(=O)O)C(=O)O`
ZINC2111575 ZINC	0.692	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1C[C@@H](N)C(=O)O)C(=O)O`
ZINC2111578 ZINC	0.692	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1C[C@@H](N)C(=O)O)C(=O)O`
ZINC2132386 ZINC	0.692	245.4 Da LogP 3.68 TPSA 21.3	✓ Ro5	✓ Clean	`COc1ccc(CNCCC2=CCCCC2)cc1`
ZINC6584728 ZINC	0.692	261.4 Da LogP 4.39 TPSA 12.0	✓ Ro5	✓ Clean	`CSc1ccc(CNCCC2=CCCCC2)cc1`
ZINC12648269 ZINC	0.690	237.3 Da LogP 0.73 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](C[C@@H](Cc1ccccc1)C(=O)O)C(=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.