Protein target profile

VK055_1196

tryptophan synthase, beta subunit

Genome: KpATCC43816 Gene: AIK79819.1 trpB 3D evidence: AlphaFold DB model + ColabFold model Metabolism 3 reactions UniProt A0A0H3GNB7

Export view

Length 397

Pocket druggability 0.945

Metabolic reactions 3

Chokepoint Yes

Direct ligand evidence 0 91 total records

Functional annotation 1 EC 4 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. Central metabolic position More central than 97.5% of genes in this genome. 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. 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: 36.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 83.333 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: 97.49 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 0.945

Structure A0A0H3GNB7

Pocket Pocket 1

P2Rank 0.931

Structure A0A0H3GNB7

Pocket Pocket 1

ColabFold model

FPocket 0.933 · Pocket 1

P2Rank 0.909 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 1726 / 4744 genomes with a hit

Prevalence 36.4%

Cross-references

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

Sequence

UniProt A0A0H3GNB7

Pathways

KEGG R02722 BioCyc TRYPSYN-RXN KEGG R02340 BioCyc RXN0-2381 KEGG R00674 BioCyc RXN0-2382

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 Benzoxazinoid biosynthesis, no isoenzyme backup detected, more central than 97.5% of genes in this genome, no human homolog detected.

Relative network centrality 97.5% more central than 97.5% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSTLLNPYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPAFQAEFTDLLKNYAGRPTALTKCRNLTDGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSYEKAHYMLGTAAGPHPFPTIVREFQRMIGEETKAQILEKEGRLPDAVIACVGGGSNAIGMFADFIEETNVGLIGVEPAGHGIESGEHGAPLKHGRVGIYFGMKSPMMQTADGQIEESYSISAGLDFPSVGPQHAFLNSTGRADYVSITDDEALDAFKALSRHEGIIPALESSHALAHALKMMRENPEKEQLLVVNLSGRGDKDIFTVHDILKARGEI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

4.2.1.20

Gene Ontology (GO)

GO:0004834 Catalysis of the reaction: L-serine + (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O.
GO:0000162 The chemical reactions and pathways resulting in the formation of L-tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; L-tryptophan is synthesized from chorismate via anthranilate.
GO:0006568 The chemical reactions and pathways involving tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
80	94	ProSitePatterns	PS00168	Tryptophan synthase beta chain pyridoxal-phosphate attachment site.
80	94	InterPro	IPR006653	Tryptophan synthase, beta chain, conserved site
23	387	CDD	cd06446	Trp-synth_B
23	387	InterPro	IPR006654	Tryptophan synthase, beta chain
6	390	SUPERFAMILY	SSF53686	Tryptophan synthase beta subunit-like PLP-dependent enzymes
6	390	InterPro	IPR036052	Tryptophan synthase beta chain-like, PALP domain superfamily
54	385	Gene3D	G3DSA:3.40.50.1100	-
54	385	InterPro	IPR036052	Tryptophan synthase beta chain-like, PALP domain superfamily
205	384	FunFam	G3DSA:3.40.50.1100:FF:000004	Tryptophan synthase beta chain
52	375	Pfam	PF00291	Pyridoxal-phosphate dependent enzyme
52	375	InterPro	IPR001926	Tryptophan synthase beta chain-like, PALP domain
9	205	Gene3D	G3DSA:3.40.50.1100	-
9	205	InterPro	IPR036052	Tryptophan synthase beta chain-like, PALP domain superfamily
8	389	NCBIfam	TIGR00263	tryptophan synthase subunit beta
8	389	InterPro	IPR006654	Tryptophan synthase, beta chain
2	391	Hamap	MF_00133	Tryptophan synthase beta chain [trpB].
2	391	InterPro	IPR023026	Tryptophan synthase beta chain/beta chain-like
1	397	PIRSF	PIRSF001413	Trp_syn_beta
1	397	InterPro	IPR023026	Tryptophan synthase beta chain/beta chain-like
7	392	PANTHER	PTHR48077	TRYPTOPHAN SYNTHASE-RELATED
7	392	InterPro	IPR023026	Tryptophan synthase beta chain/beta chain-like
73	204	FunFam	G3DSA:3.40.50.1100:FF:000001	Tryptophan synthase beta chain

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

0.945

Likely same site as P2Rank 1 0.9 Å 27 shared residues 100% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #7

0.568

Likely same site as P2Rank 3 3.1 Å 11 shared residues 100% of smaller site

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.931

Likely same site as FPocket 1 0.9 Å 27 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.173

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.093

Likely same site as FPocket 7 3.1 Å 11 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.088

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.029

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.909

Likely same site as FPocket 1 0.6 Å 25 shared residues 96% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.193

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.086

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.069

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.02

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_A0A0H3GNB7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1196	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.

91 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 41 records from similar proteins

Structural ligands 41 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0JO PDB via homolog 316.2 Da · LogP 0.72 · TPSA 149.5 Open detail RCSB PDB

13P PDB via homolog Detail RCSB PDB

1D0 PDB via homolog Detail RCSB PDB

78U PDB via homolog Detail RCSB PDB

79V 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
0JO RCSB PDB	4HPX	P0A2K1	316.2 Da LogP 0.72 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/C(=C)C(=O)O)O`
13P RCSB PDB	1K8Y	P0A2K1	170.1 Da LogP -1.34 TPSA 104.1	✓ Ro5	✓ Clean	`C(C(=O)COP(=O)(O)O)O`
1D0 RCSB PDB	4HPJ	P0A2K1	425.3 Da LogP 1.55 TPSA 181.8	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)C/N=C(\CNc2ccccc2O)/C(…`
78U RCSB PDB	5T6M	Q8U093	218.3 Da LogP 1.68 TPSA 79.1	✓ Ro5	✓ Clean	`C[C@@H](c1c[nH]c2c1cccc2)[C@@H](C(=O)O)N`
79V RCSB PDB	5TCI	P9WFX9	282.3 Da LogP 2.43 TPSA 56.0	✓ Ro5	✓ Clean	`c1ccc(c(c1)c2ccc(cc2)C3C(NC3C#N)CO)F`
7MN RCSB PDB	3PR2	P0A2K1	436.4 Da LogP -0.07 TPSA 153.5	1 viol.	✓ Clean	`CC1=C(/C(=C\[NH+]=C(/C[N@@]2CCc3c2cccc3)\C(=O)O…`
AQ3 RCSB PDB	4KKX	P0A2K1	427.4 Da LogP 1.07 TPSA 181.5	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@H](CNc2ccccc2O)C(…`
BZI RCSB PDB	6X0C	P0A2K1	118.1 Da LogP 1.56 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc2c(c1)[nH]cn2`
F6F RCSB PDB	4KKX	P0A2K1	329.2 Da LogP 1.42 TPSA 105.1	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)NCCOP(=O)(O)O)OC(F)(F)F`
F9F RCSB PDB	3PR2	P0A2K1	365.2 Da LogP 0.97 TPSA 122.2	✓ Ro5	✓ Clean	`c1cc(ccc1OC(F)(F)F)S(=O)(=O)NCCOP(=O)(O)O`
FEJ RCSB PDB	6CUT	Q8U093	376.3 Da LogP 0.59 TPSA 169.8	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/[C@@H]([C@H](C(C)…`
FEV RCSB PDB	6CUZ	Q8U093	344.3 Da LogP 1.50 TPSA 149.5	✓ Ro5	✓ Clean	`CC/C=C(\C(=O)O)/N=C/c1c(cnc(c1O)C)COP(=O)(O)O`
FIP RCSB PDB	1A50	P0A2K1	273.2 Da LogP 2.35 TPSA 82.6	✓ Ro5	✓ Clean	`c1cc2c(cc1F)c(c[nH]2)CCCOP(=O)(O)O`
G3P RCSB PDB	2TSY	P0A2K1	172.1 Da LogP -1.55 TPSA 107.2	✓ Ro5	✓ Clean	`C([C@H](COP(=O)(O)O)O)O`
H9V RCSB PDB	6UAP	P9WFX9	336.7 Da LogP 4.20 TPSA 35.8	✓ Ro5	✓ Clean	`c1cc(ccc1c2c(cc(cc2F)Cl)F)C3C(NC3C#N)CF`
HDJ RCSB PDB	6DWE	P9WFX9	316.3 Da LogP 3.86 TPSA 35.8	✓ Ro5	✓ Clean	`Cc1cc(c(c(c1)F)c2ccc(cc2)C3C(NC3C#N)CF)F`
HE1 RCSB PDB	1C29	P0A2K1	260.3 Da LogP 2.57 TPSA 77.8	✓ Ro5	✓ Clean	`c1ccc(c(c1)O)SCC\C=C\P(=O)(O)O`
HF1 RCSB PDB	1C9D	P0A2K1	278.2 Da LogP 2.70 TPSA 77.8	✓ Ro5	✓ Clean	`c1cc(c(cc1F)SCCC=CP(=O)(O)O)O`
HPF RCSB PDB	1TJP	P0A2K1	279.2 Da LogP -0.41 TPSA 139.5	1 viol.	✓ Clean	`c1ccc(c(c1)N[C@@H]([C@@H](COP(=O)(O)O)O)O)O`
HSP RCSB PDB	1CW2	P0A2K1	278.3 Da LogP 1.46 TPSA 94.8	✓ Ro5	✓ Clean	`c1ccc(c(c1)O)[S@](=O)CCCCP(=O)(O)O`
IAD RCSB PDB	1K3U	P0A2K1	290.3 Da LogP 0.75 TPSA 119.5	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)CC(=O)N[C@@H](CC(=O)O)C(=O)O`
IAG RCSB PDB	1K8Z	P0A2K1	232.2 Da LogP 0.91 TPSA 82.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)CC(=O)NCC(=O)O`
IDM RCSB PDB	3CEP	P0A2K1	119.2 Da LogP 1.65 TPSA 12.0	✓ Ro5	✓ Clean	`c1ccc2c(c1)CCN2`
IGP RCSB PDB	2RH9	P0A2K1	287.2 Da LogP 0.67 TPSA 123.0	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)[C@@H]([C@@H](COP(=O)(O)O)O…`
IPL RCSB PDB	1BEU	P0A2K1	255.2 Da LogP 2.21 TPSA 82.6	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)CCCOP(=O)(O)O`
KOU RCSB PDB	6DZO	P0A2K1	334.2 Da LogP -0.43 TPSA 169.8	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/C(CO)C(=O)O)O`
MH6 RCSB PDB	3CEP	P0A2K1	103.1 Da LogP -0.92 TPSA 81.4	✓ Ro5	✓ Clean	`[H]/N=C(\CO)/C(=O)O`
MLA RCSB PDB	6E9P	P9WFX9	104.1 Da LogP -0.45 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)O)C(=O)O`
MLI RCSB PDB	5TCG	P9WFX9	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MLT RCSB PDB	6UAP	P9WFX9	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
NH4 RCSB PDB	4XUG	P0A2K1	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
NHP RCSB PDB	1CX9	P0A2K1	261.3 Da LogP 2.32 TPSA 83.6	✓ Ro5	✓ Clean	`c1ccc(c(c1)N)SCCCCP(=O)(O)O`
P1T RCSB PDB	5OCW	P9WFX9	318.2 Da LogP 0.39 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNC(=C)C(=O)O)O`
PG5 RCSB PDB	4HT3	P0A2K1	178.2 Da LogP 0.31 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOC`
PLR RCSB PDB	4QYS	Q97TX6	233.2 Da LogP 1.01 TPSA 99.9	✓ Ro5	✓ Clean	`Cc1c(cnc(c1O)C)COP(=O)(O)O`
PLS RCSB PDB	1BEU	P0A2K1	336.2 Da LogP -0.76 TPSA 169.4	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CO)C(=O)O)O`
PLT RCSB PDB	2TYS	P0A2K1	433.4 Da LogP 2.30 TPSA 165.3	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)\C=N\[C@@H](Cc2c[nH]c3…`
PZJ RCSB PDB	6USA	P9WFX9	330.8 Da LogP 0.62 TPSA 60.9	✓ Ro5	✓ Clean	`c1ccc(c(c1)N2CCN(CC2)[C@H]3CS(=O)(=O)C[C@@H]3O)…`
PZV RCSB PDB	6U6C	P9WFX9	334.4 Da LogP 1.94 TPSA 66.5	✓ Ro5	✓ Clean	`CNS(=O)(=O)c1ccc2c(c1)CCN2C(=O)c3ccccc3F`
SEP RCSB PDB	4QYS	Q97TX6	185.1 Da LogP -1.49 TPSA 130.1	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)N)OP(=O)(O)O`
V41 RCSB PDB	6XIN	P0A2K1	205.2 Da LogP 0.56 TPSA 117.7	✓ Ro5	Alert	`[H]/N=C(/[C@H](C(=O)N)/N=N/c1ccccc1)\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
ZINC1692489 ZINC	1.000	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC2047144 ZINC	1.000	261.3 Da LogP 2.32 TPSA 83.6	✓ Ro5	✓ Clean	`Nc1ccccc1SCCCCP(=O)(O)O`
ZINC32743325 ZINC	1.000	330.8 Da LogP 0.62 TPSA 60.9	✓ Ro5	✓ Clean	`O=S1(=O)C[C@@H](O)[C@@H](N2CCN(c3ccccc3Cl)CC2)C1`
ZINC32743327 ZINC	1.000	330.8 Da LogP 0.62 TPSA 60.9	✓ Ro5	✓ Clean	`O=S1(=O)C[C@H](O)[C@@H](N2CCN(c3ccccc3Cl)CC2)C1`
ZINC32743329 ZINC	1.000	330.8 Da LogP 0.62 TPSA 60.9	✓ Ro5	✓ Clean	`O=S1(=O)C[C@@H](O)[C@H](N2CCN(c3ccccc3Cl)CC2)C1`
ZINC32743330 ZINC	1.000	330.8 Da LogP 0.62 TPSA 60.9	✓ Ro5	✓ Clean	`O=S1(=O)C[C@@H](N2CCN(c3ccccc3Cl)CC2)[C@@H](O)C1`
ZINC4530388 ZINC	1.000	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC56756 ZINC	1.000	290.3 Da LogP 0.75 TPSA 119.5	✓ Ro5	✓ Clean	`O=C(O)C[C@H](NC(=O)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC56757 ZINC	1.000	290.3 Da LogP 0.75 TPSA 119.5	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](NC(=O)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC5701172 ZINC	1.000	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC57380 ZINC	1.000	232.2 Da LogP 0.91 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)Cc1c[nH]c2ccccc12`
ZINC58290514 ZINC	1.000	334.4 Da LogP 1.94 TPSA 66.5	✓ Ro5	✓ Clean	`CNS(=O)(=O)c1ccc2c(c1)CCN2C(=O)c1ccccc1F`
ZINC5997861 ZINC	1.000	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC83315 ZINC	1.000	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC83317 ZINC	1.000	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC3070964 ZINC	0.805	361.4 Da LogP 3.00 TPSA 98.0	✓ Ro5	✓ Clean	`O=C(Cc1c[nH]c2ccccc12)N[C@@H](Cc1c[nH]c2ccccc12…`
ZINC3070965 ZINC	0.805	361.4 Da LogP 3.00 TPSA 98.0	✓ Ro5	✓ Clean	`O=C(Cc1c[nH]c2ccccc12)N[C@H](Cc1c[nH]c2ccccc12)…`
ZINC14517334 ZINC	0.791	304.3 Da LogP 1.14 TPSA 119.5	✓ Ro5	✓ Clean	`O=C(O)CC[C@@H](NC(=O)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC4090458 ZINC	0.791	304.3 Da LogP 1.14 TPSA 119.5	✓ Ro5	✓ Clean	`O=C(O)CC[C@H](NC(=O)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC100061983 ZINC	0.788	205.2 Da LogP 0.56 TPSA 117.7	✓ Ro5	Alert	`N=C(N)[C@@H](/N=N/c1ccccc1)C(N)=O`
ZINC100137008 ZINC	0.788	205.2 Da LogP 0.56 TPSA 117.7	✓ Ro5	Alert	`N=C(N)[C@H](/N=N\c1ccccc1)C(N)=O`
ZINC12671074 ZINC	0.788	205.2 Da LogP 0.56 TPSA 117.7	✓ Ro5	Alert	`N=C(N)[C@@H](N=Nc1ccccc1)C(N)=O`
ZINC57675665 ZINC	0.788	205.2 Da LogP 0.56 TPSA 117.7	✓ Ro5	Alert	`N=C(N)[C@H](/N=N/c1ccccc1)C(N)=O`
ZINC8034690 ZINC	0.788	205.2 Da LogP 0.56 TPSA 117.7	✓ Ro5	Alert	`N=C(N)[C@H](N=Nc1ccccc1)C(N)=O`
ZINC11889378 ZINC	0.786	260.3 Da LogP 1.69 TPSA 82.2	✓ Ro5	✓ Clean	`CC[C@@H](NC(=O)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC11889380 ZINC	0.786	260.3 Da LogP 1.69 TPSA 82.2	✓ Ro5	✓ Clean	`CC[C@H](NC(=O)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC58245588 ZINC	0.784	352.4 Da LogP 2.08 TPSA 66.5	✓ Ro5	✓ Clean	`CNS(=O)(=O)c1ccc2c(c1)CCN2C(=O)c1ccc(F)cc1F`
ZINC58283400 ZINC	0.784	368.8 Da LogP 2.59 TPSA 66.5	✓ Ro5	✓ Clean	`CNS(=O)(=O)c1ccc2c(c1)CCN2C(=O)c1ccc(Cl)cc1F`
ZINC519516057 ZINC	0.780	350.8 Da LogP 2.45 TPSA 66.5	✓ Ro5	✓ Clean	`CNS(=O)(=O)c1ccc2c(c1)CCN2C(=O)c1ccccc1Cl`
ZINC58293030 ZINC	0.780	330.4 Da LogP 2.11 TPSA 66.5	✓ Ro5	✓ Clean	`CNS(=O)(=O)c1ccc2c(c1)CCN2C(=O)c1ccccc1C`
ZINC205262 ZINC	0.778	264.3 Da LogP 3.03 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(Cc1c[nH]c2ccccc12)NCc1ccccc1`
ZINC4899521 ZINC	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC57505 ZINC	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC5423113 ZINC	0.769	246.3 Da LogP 1.30 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)CCc1c[nH]c2ccccc12`
ZINC389660 ZINC	0.767	322.4 Da LogP 2.52 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(Cc1c[nH]c2ccccc12)N[C@@H](Cc1ccccc1)C(=O)O`
ZINC389661 ZINC	0.767	322.4 Da LogP 2.52 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(Cc1c[nH]c2ccccc12)N[C@H](Cc1ccccc1)C(=O)O`
ZINC56758 ZINC	0.767	288.3 Da LogP 2.33 TPSA 82.2	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC56759 ZINC	0.767	288.3 Da LogP 2.33 TPSA 82.2	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC2566035 ZINC	0.757	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](CCc1c[nH]c2ccccc12)C(=O)O`
ZINC6864822 ZINC	0.757	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](CCc1c[nH]c2ccccc12)C(=O)O`
ZINC4090499 ZINC	0.756	318.3 Da LogP 1.53 TPSA 119.5	✓ Ro5	✓ Clean	`O=C(O)C[C@H](NC(=O)CCCc1c[nH]c2ccccc12)C(=O)O`
ZINC261723012 ZINC	0.750	296.3 Da LogP 1.94 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(Cc1c[nH]c2ccccc12)N[C@H](CC(F)F)C(=O)O`
ZINC261723018 ZINC	0.750	296.3 Da LogP 1.94 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(Cc1c[nH]c2ccccc12)N[C@@H](CC(F)F)C(=O)O`
ZINC6624307 ZINC	0.744	246.3 Da LogP 1.30 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(O)CCNC(=O)Cc1c[nH]c2ccccc12`
ZINC1690614 ZINC	0.743	233.2 Da LogP 1.50 TPSA 90.4	✓ Ro5	✓ Clean	`O=C(O)C(Cc1c[nH]c2ccccc12)C(=O)O`
ZINC1529618 ZINC	0.739	246.2 Da LogP -2.17 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(OC[C@@H](O)CO)OC[C@H](O)CO`
ZINC1529620 ZINC	0.739	246.2 Da LogP -2.17 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(OC[C@@H](O)CO)OC[C@@H](O)CO`
ZINC34764844 ZINC	0.733	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
ZINC264242 ZINC	0.732	293.4 Da LogP 2.35 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCc1ccccc1`
ZINC8879429 ZINC	0.732	260.3 Da LogP 1.69 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)CCCc1c[nH]c2ccccc12`

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.