Protein target profile

KP13_04672

Phenylalanyl-tRNA synthetase beta chain

Genome: KpKP13 Gene: AHE44068.1 pheT 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GUX6

Export view

Length 795

Pocket druggability 0.821

Direct ligand evidence 0 54 total records

Functional annotation 1 EC 7 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: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.82, P2Rank 0.88). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. 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 0.88. 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 (%): 22.716 Lower values reduce human off-target concern.
Human E-value: 5.5e-10
Gut microbiome similarity: 3.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.453 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: 95.58 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 0.821

Structure A0A0H3GUX6

Pocket Pocket 1

P2Rank 0.876

Structure A0A0H3GUX6

Pocket Pocket 1

ColabFold model

FPocket 0.566 · Pocket 2

P2Rank 0.799 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 153 / 4744 genomes with a hit

Prevalence 3.2%

Cross-references

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

Sequence

UniProt A0A0H3GUX6

Sequence

Primary amino-acid sequence viewer.

MKFSELWLREWVNPAIDSEALSDQITMAGLEVDGVEPVAGSFNGVVVGEVVECGQHPNADKLRVTKVNVGGERLLDIVCGAPNCRQGLKVAVATIGAVLPGDFKIKAAKLRGEPSEGMLCSFSELGISDDHSGIIELPADAPIGTDIREYLKLDDNTIEISVTPNRADCLGIIGVARDVAVLNKAPLNAPEITPVAATIDDVLPIQVDAPQACPRYLGRVVKGINVKAPTPLWMKEKLRRCGIRSIDAVVDVTNYVLLELGQPMHAFDRDRIEGGIVVRMAKEGETLVLLDGSEAKLDSDTLVIADHNKALAMGGIFGGEHSGVNDETQNVLLECAFFSPLSITGRARRHGLHTDASHRYERGVDPALQYKALERATRLLIDLCGGEAGPVIDVTSKENLPTRATITLRRSKLDRLIGHHIADAQVTDILQRLGCEVTVGEGEWQAVAPSWRFDMEIEEDLVEEVARVYGYNNIPDEPVQAGLIMGTHREADLSLKRVKTLLNDKGYQEVITYSFVDPKVQQLIHAGEEALILPSPISSEMSAMRLSLWTGLLGTVVYNQNRQQSRVRIFESGLRFVPDTNAPLGIRQDVMLAGAICGNRYEEHWTLAKETVDFYDLKGDLEAVLDLTGKLADIEFRAEATTALHPGQSAAIYLKGERIGFIGVVHPELERKLDLNGRTLVFELEWNKLADRVVPQARDISRFPANRRDIAVLVAENVAAADVLAECKKVGVNQVVGVNLFDVYRGKGVAEGYKSLAISLILQDTSRTLEEEEIAATVARCVEALKERFQASLRD

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

6.1.1.20

Gene Ontology (GO)

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:0000287 Binding to a magnesium (Mg) ion.
GO:0003723 Binding to an RNA molecule or a portion thereof.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0009328 An enzyme complex that catalyzes the ligation of phenylalanine to tRNA(Phe), forming L-phenylalanyl-tRNA(Phe).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

53 records

Show feature table

Start	End	DB	Term	Name
45	145	Pfam	PF01588	Putative tRNA binding domain
45	145	InterPro	IPR002547	tRNA-binding domain
1	788	Hamap	MF_00283	Phenylalanine--tRNA ligase beta subunit [pheT].
1	788	InterPro	IPR004532	Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type
696	794	SUPERFAMILY	SSF54991	Anticodon-binding domain of PheRS
696	794	InterPro	IPR036690	Ferrodoxin-fold anticodon-binding domain superfamily
401	476	ProSiteProfiles	PS51483	B5 domain profile.
401	476	InterPro	IPR005147	tRNA synthetase, B5-domain
53	147	CDD	cd02796	tRNA_bind_bactPheRS
53	147	InterPro	IPR033714	Phenylalanly tRNA synthetase, tRNA-binding-domain
196	397	FunFam	G3DSA:3.50.40.10:FF:000001	Phenylalanine--tRNA ligase beta subunit
475	685	Pfam	PF17759	Phenylalanyl tRNA synthetase beta chain CLM domain
475	685	InterPro	IPR041616	Phenylalanyl tRNA synthetase beta chain, core domain
404	475	SUPERFAMILY	SSF46955	Putative DNA-binding domain
404	475	InterPro	IPR009061	Putative DNA-binding domain superfamily
701	794	Pfam	PF03147	Ferredoxin-fold anticodon binding domain
701	794	InterPro	IPR005121	Ferrodoxin-fold anticodon-binding domain
403	471	SMART	SM00874	B5_2
403	471	InterPro	IPR005147	tRNA synthetase, B5-domain
212	385	SMART	SM00873	B3_4_2
212	385	InterPro	IPR005146	B3/B4 tRNA-binding domain
401	475	Gene3D	G3DSA:3.30.56.10	-
702	795	Gene3D	G3DSA:3.30.70.380	-
702	795	InterPro	IPR036690	Ferrodoxin-fold anticodon-binding domain superfamily
485	693	Gene3D	G3DSA:3.30.930.10	Bira Bifunctional Protein; Domain 2
485	693	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
1	794	NCBIfam	TIGR00472	phenylalanine--tRNA ligase subunit beta
1	794	InterPro	IPR004532	Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type
702	795	FunFam	G3DSA:3.30.70.380:FF:000001	Phenylalanine--tRNA ligase beta subunit
4	686	PANTHER	PTHR10947	PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47
4	686	InterPro	IPR045060	Phenylalanine-tRNA ligase, class IIc, beta subunit
487	692	FunFam	G3DSA:3.30.930.10:FF:000022	Phenylalanine--tRNA ligase beta subunit
467	690	SUPERFAMILY	SSF55681	Class II aaRS and biotin synthetases
467	690	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
39	148	ProSiteProfiles	PS50886	tRNA-binding domain profile.
39	148	InterPro	IPR002547	tRNA-binding domain
7	180	Gene3D	G3DSA:3.30.56.10	-
39	154	Gene3D	G3DSA:2.40.50.140	-
39	154	InterPro	IPR012340	Nucleic acid-binding, OB-fold
197	395	Gene3D	G3DSA:3.50.40.10	-
197	395	InterPro	IPR020825	Phenylalanyl-tRNA synthetase-like, B3/B4
39	154	FunFam	G3DSA:2.40.50.140:FF:000045	Phenylalanine--tRNA ligase beta subunit
35	197	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
35	197	InterPro	IPR012340	Nucleic acid-binding, OB-fold
195	396	SUPERFAMILY	SSF56037	PheT/TilS domain
701	794	SMART	SM00896	FDX_ACB_2
402	475	FunFam	G3DSA:3.30.56.10:FF:000002	Phenylalanine--tRNA ligase beta subunit
212	385	Pfam	PF03483	B3/4 domain
406	471	Pfam	PF03484	tRNA synthetase B5 domain
406	471	InterPro	IPR005147	tRNA synthetase, B5-domain
701	794	ProSiteProfiles	PS51447	Ferredoxin-fold anticodon binding (FDX-ACB) domain profile.
495	689	CDD	cd00769	PheRS_beta_core
495	689	InterPro	IPR041616	Phenylalanyl tRNA synthetase beta chain, core domain

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

0.821

Likely same site as P2Rank 5 6.8 Å 6 shared residues 67% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #3

0.475

Likely same site as P2Rank 1 0.8 Å 22 shared residues 96% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 3 FPocket #32

0.232

Show in viewer

Surrounding area

Site 4 FPocket #6

0.227

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.876

Likely same site as FPocket 3 0.8 Å 22 shared residues 96% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.473

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.15

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.098

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.097

Likely same site as FPocket 1 6.8 Å 6 shared residues 67% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:454-454

UniProt: Binding site:460-460

UniProt: Binding site:463-463

UniProt: Binding site:464-464

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.799

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.462

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.166

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.069

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.062

Show in viewer

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_A0A0H3GUX6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04672	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

DAH PDB via homolog 197.2 Da · LogP 0.05 · TPSA 103.8 Open detail RCSB PDB

MTY PDB via homolog Detail RCSB PDB

PUY PDB via homolog Detail RCSB PDB

TAM PDB via homolog Detail RCSB PDB

ZINC53147178 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
DAH RCSB PDB	3TEH	P27002	197.2 Da LogP 0.05 TPSA 103.8	✓ Ro5	Alert	`c1cc(c(cc1C[C@@H](C(=O)O)N)O)O`
MTY RCSB PDB	3HFZ	Q5SGX1	181.2 Da LogP 0.35 TPSA 83.5	✓ Ro5	✓ Clean	`c1cc(cc(c1)O)C[C@@H](C(=O)O)N`
PUY RCSB PDB	4TVA	Q5SGX1	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`CN(C)c1c2c(ncn1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H]…`
TAM RCSB PDB	3ICA	Q7MXR4	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`

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
ZINC53147178 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@@H](CO)O[C@@H…`
ZINC53147179 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@@H](CO)O[C@@H]…`
ZINC58994963 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@@H]…`
ZINC59065899 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](O)[C@@H](n…`
ZINC59817042 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@H](…`
ZINC59817043 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N[C@H]2[C@H](O)[C@@H](n3…`
ZINC59817045 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N[C@H]2[C@H](O)[C@H](n3c…`
ZINC61389312 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@@H](CO)O[C@H](…`
ZINC71789712 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@@H](CO)O[C@H]…`
ZINC73333306 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@H](n…`
ZINC73333309 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@@H](…`
ZINC73333313 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@H](N)C(=O)N[C@H]2[C@H](O)[C@@H](n3c…`
ZINC73333316 ZINC	1.000	471.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`COc1ccc(C[C@H](N)C(=O)N[C@H]2[C@H](O)[C@H](n3cn…`
ZINC4830897 ZINC	0.829	443.5 Da LogP -1.28 TPSA 183.7	1 viol.	✓ Clean	`COc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@H](n…`
ZINC4830899 ZINC	0.829	443.5 Da LogP -1.28 TPSA 183.7	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@H](…`
ZINC4830900 ZINC	0.829	443.5 Da LogP -1.28 TPSA 183.7	1 viol.	✓ Clean	`COc1ccc(C[C@H](N)C(=O)N[C@H]2[C@H](CO)O[C@H](n3…`
ZINC4830901 ZINC	0.829	443.5 Da LogP -1.28 TPSA 183.7	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N[C@H]2[C@H](CO)O[C@H](n…`
ZINC1775953634 ZINC	0.824	495.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`C#CCOc1ccc(C[C@H](N)C(=O)N[C@H]2[C@@H](CO)O[C@@…`
ZINC205891530 ZINC	0.824	495.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`C#CCOc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@@H](CO)O[C@…`
ZINC221530727 ZINC	0.824	495.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`C#CCOc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@…`
ZINC221530830 ZINC	0.824	495.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`C#CCOc1ccc(C[C@@H](N)C(=O)N[C@H]2[C@H](O)[C@@H]…`
ZINC222589180 ZINC	0.824	495.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`C#CCOc1ccc(C[C@H](N)C(=O)N[C@H]2[C@@H](CO)O[C@@…`
ZINC669678878 ZINC	0.824	495.5 Da LogP -0.79 TPSA 160.9	1 viol.	✓ Clean	`C#CCOc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](O)[C@@H…`
ZINC403598 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC403599 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC1834294 ZINC	0.793	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	0.793	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	0.793	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`
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`
ZINC2512061 ZINC	0.774	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@H](N)C(=O)O)ccc2O)…`
ZINC53188912 ZINC	0.753	485.5 Da LogP -0.45 TPSA 152.1	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N(C)[C@@H]2[C@H](CO)O[C@…`
ZINC53188914 ZINC	0.753	485.5 Da LogP -0.45 TPSA 152.1	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N(C)[C@@H]2[C@H](CO)O[C@…`
ZINC53188917 ZINC	0.753	485.5 Da LogP -0.45 TPSA 152.1	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N(C)[C@H]2[C@H](O)[C@@H]…`
ZINC53188920 ZINC	0.753	485.5 Da LogP -0.45 TPSA 152.1	1 viol.	✓ Clean	`COc1ccc(C[C@@H](N)C(=O)N(C)[C@H]2[C@H](O)[C@H](…`
ZINC39351856 ZINC	0.741	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…`
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`
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`
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`
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`
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`

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.