Protein target profile

VK055_3750

translation elongation factor Tu

Genome: KpATCC43816 Gene: AIK82305.1 tuf2 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GLP8

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Length 394

Pocket druggability 0.781

Direct ligand evidence 0 70 total records

Functional annotation 1 EC 8 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

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

Main supporting evidence

Strong predicted binding pocket FPocket selected-pocket score 0.78. This is a computational pocket signal, not binding validation. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 20 structural and 0 bioactivity records.

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 (%): 81.25 Lower values reduce human off-target concern.
Human E-value: 1.64e-09
Gut microbiome similarity: 69.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 98.223 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: 92.33 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 0.781

Structure A0A0H3GLP8

Pocket Pocket 9

P2Rank 0.383

Structure A0A0H3GLP8

Pocket Pocket 1

ColabFold model

FPocket 0.726 · Pocket 21

P2Rank 0.466 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 3316 / 4744 genomes with a hit

Prevalence 69.9%

Cross-references

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

Sequence

UniProt A0A0H3GLP8

Sequence

Primary amino-acid sequence viewer.

MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

3.6.5.3

Gene Ontology (GO)

GO:0003746 Functions in chain elongation during polypeptide synthesis at the ribosome.
GO:0005525 Binding to GTP, guanosine triphosphate.
GO:0006414 The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.
GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0032045 A protein complex that stimulates the exchange of guanyl nucleotides associated with a GTPase.
GO:0097216 Binding to guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions.
GO:0000287 Binding to a magnesium (Mg) ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

44 records

Show feature table

Start	End	DB	Term	Name
300	389	CDD	cd03707	EFTU_III
298	392	Pfam	PF03143	Elongation factor Tu C-terminal domain
298	392	InterPro	IPR004160	Translation elongation factor EFTu/EF1A, C-terminal
13	148	NCBIfam	TIGR00231	small GTP-binding protein domain
13	148	InterPro	IPR005225	Small GTP-binding protein domain
14	27	PRINTS	PR00315	GTP-binding elongation factor signature
14	27	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
58	66	PRINTS	PR00315	GTP-binding elongation factor signature
58	66	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
131	140	PRINTS	PR00315	GTP-binding elongation factor signature
131	140	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
94	105	PRINTS	PR00315	GTP-binding elongation factor signature
94	105	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
78	88	PRINTS	PR00315	GTP-binding elongation factor signature
78	88	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
1	203	Gene3D	G3DSA:3.40.50.300	-
1	203	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
298	393	SUPERFAMILY	SSF50465	EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
298	393	InterPro	IPR009001	Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal
11	203	CDD	cd01884	EF_Tu
11	203	InterPro	IPR041709	Elongation factor Tu (EF-Tu), GTP-binding domain
1	393	NCBIfam	TIGR00485	elongation factor Tu
1	393	InterPro	IPR004541	Translation elongation factor EFTu/EF1A, bacterial/organelle
206	334	FunFam	G3DSA:2.40.30.10:FF:000001	Elongation factor Tu
211	297	CDD	cd03697	EFTU_II
211	297	InterPro	IPR033720	Elongation factor Tu, domain 2
1	394	Hamap	MF_00118_B	Elongation factor Tu [tuf].
1	394	InterPro	IPR004541	Translation elongation factor EFTu/EF1A, bacterial/organelle
1	203	FunFam	G3DSA:3.40.50.300:FF:000003	Elongation factor Tu
10	198	Pfam	PF00009	Elongation factor Tu GTP binding domain
10	198	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
205	301	SUPERFAMILY	SSF50447	Translation proteins
205	301	InterPro	IPR009000	Translation protein, beta-barrel domain superfamily
206	334	Gene3D	G3DSA:2.40.30.10	Translation factors
338	393	Gene3D	G3DSA:2.40.30.10	Translation factors
4	393	PANTHER	PTHR43721	ELONGATION FACTOR TU-RELATED
225	293	Pfam	PF03144	Elongation factor Tu domain 2
225	293	InterPro	IPR004161	Translation elongation factor EFTu-like, domain 2
51	66	ProSitePatterns	PS00301	Translational (tr)-type guanine nucleotide-binding (G) domain signature.
51	66	InterPro	IPR031157	Tr-type G domain, conserved site
6	219	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
6	219	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
10	204	ProSiteProfiles	PS51722	Translational (tr)-type guanine nucleotide-binding (G) domain profile.
10	204	InterPro	IPR000795	Translational (tr)-type GTP-binding 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.

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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 #9

0.781

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Surrounding area

Site 2 FPocket #3

0.209

Likely same site as P2Rank 2 4.0 Å 11 shared residues 79% of smaller site

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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

0.383

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Surrounding area

Site 2 P2Rank #2

0.368

Likely same site as FPocket 3 4.0 Å 11 shared residues 79% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.104

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Surrounding area

Site 4 P2Rank #4

0.043

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Surrounding area

Site 5 P2Rank #5

0.012

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Surrounding area

Residue sets

UniProt: Binding site:136-139

UniProt: Binding site:19-26

UniProt: Binding site:26-26

UniProt: Binding site:81-85

Binding pockets · FPocket

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

Site 1 FPocket #21

0.726

Likely same site as P2Rank 1 7.0 Å 10 shared residues 77% of smaller site

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Surrounding area

Site 2 FPocket #1

0.567

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Surrounding area

Site 3 FPocket #9

0.27

Likely same site as P2Rank 1 3.6 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 4 FPocket #14

0.228

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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

0.466

Likely same site as FPocket 9 3.6 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.415

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Surrounding area

Site 3 P2Rank #3

0.051

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Surrounding area

Site 4 P2Rank #4

0.028

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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_A0A0H3GLP8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3750	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.

70 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 20 records from similar proteins

Structural ligands 20 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

14J PDB via homolog 191.0 Da · LogP 1.74 · TPSA 50.4 Open detail RCSB PDB

1MG PDB via homolog Detail RCSB PDB

5MU PDB via homolog Detail RCSB PDB

A PDB via homolog Detail RCSB PDB

APR 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
14J RCSB PDB	4H9G	P60338	191.0 Da LogP 1.74 TPSA 50.4	✓ Ro5	✓ Clean	`c1cc(oc1C(=O)O)Br`
1MG RCSB PDB	5AFI	P0CE48	377.3 Da LogP -2.56 TPSA 195.2	1 viol.	✓ Clean	`CN1C(=O)c2c(n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
5MU RCSB PDB	5AFI	P0CE48	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
A RCSB PDB	4V5G	Q5SHN6	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
APR RCSB PDB	2P8Z	P60339	559.3 Da LogP -3.28 TPSA 291.5	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
C RCSB PDB	4V5P	Q5SHN6	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
ENX RCSB PDB	1OB5	Q01698	702.6 Da LogP 3.60 TPSA 213.9	2 viol.	✓ Clean	`CC/C=C/[C@H]([C@H]([C@@H](CC(=O)[C@H]([C@@H]([C…`
GCP RCSB PDB	5UYK	P0CE47	521.2 Da LogP -2.22 TPSA 289.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GLV RCSB PDB	2HCJ	Q1R5Y2	74.0 Da LogP -0.73 TPSA 54.4	✓ Ro5	✓ Clean	`C(=O)C(=O)O`
GNP RCSB PDB	4PC6	A0A0M3KKV1	522.2 Da LogP -2.76 TPSA 301.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
KIR RCSB PDB	5AFI	P0CE48	797.0 Da LogP 3.07 TPSA 228.1	3 viol.	✓ Clean	`CC[C@H](C(=O)NC\C=C\C=C(/C)\[C@H]([C@@H](C)[C@H…`
MAU RCSB PDB	4V68	P60339	811.0 Da LogP 3.09 TPSA 217.2	3 viol.	✓ Clean	`CC[C@H](C(=O)NC\C=C\C=C(/C)\[C@H]([C@@H](C)[C@H…`
NH4 RCSB PDB	4H9G	P60338	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
OGA RCSB PDB	4IW3	Q88QP8	147.1 Da LogP -1.73 TPSA 103.7	✓ Ro5	✓ Clean	`C(C(=O)O)NC(=O)C(=O)O`
PHA RCSB PDB	4V68	P60339	149.2 Da LogP 0.76 TPSA 43.1	✓ Ro5	✓ Clean	`c1ccc(cc1)C[C@@H](C=O)N`
PSU RCSB PDB	5AFI	P0CE48	324.2 Da LogP -2.67 TPSA 182.2	1 viol.	✓ Clean	`C1=C(C(=O)NC(=O)N1)[C@H]2[C@@H]([C@@H]([C@H](O2…`
PUL RCSB PDB	4PC7	P0CE47	839.0 Da LogP 4.82 TPSA 198.5	2 viol.	✓ Clean	`C[C@@H]1[C@@H]([C@@H]([C@H]([C@@H](O1)O[C@@H](C…`
PXN RCSB PDB	3MMP	P0CE48	368.5 Da LogP -0.44 TPSA 117.8	✓ Ro5	✓ Clean	`C[C@H](COCC(COC[C@@H](C)O)(COC[C@@H](C)O)COC[C@…`
SO1 RCSB PDB	2P8Z	P60339	494.6 Da LogP 2.49 TPSA 122.5	✓ Ro5	✓ Clean	`C[C@@H]1CC[C@@H]2[C@@H]1C[C@@]3([C@H]4CC([C@@]3…`
TAC RCSB PDB	2HCJ	Q1R5Y2	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`C[C@]1(c2cccc(c2C(=O)C3=C([C@]4([C@@H](C[C@@H]3…`

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
ZINC11525121 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC13515793 ZINC	1.000	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H]2…`
ZINC18202167 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC20410403 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC21984166 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC239173596 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4059755 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4215819 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3C…`
ZINC43771554 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4807269 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC575338663 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C(…`
ZINC84441937 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC13518650 ZINC	0.837	418.2 Da LogP -2.31 TPSA 217.8	1 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[C…`
ZINC104869865 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC65748564 ZINC	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC65748567 ZINC	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC77312680 ZINC	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC13519607 ZINC	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)OP…`
ZINC31298140 ZINC	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168754 ZINC	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168756 ZINC	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC28630683 ZINC	0.800	444.4 Da LogP 0.84 TPSA 182.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(=N)O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC35051264 ZINC	0.800	444.4 Da LogP 0.84 TPSA 182.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(=N)O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC71769623 ZINC	0.793	417.4 Da LogP -0.78 TPSA 198.6	1 viol.	✓ Clean	`C[C@@]1(O)c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C…`
ZINC71769624 ZINC	0.793	417.4 Da LogP -0.78 TPSA 198.6	1 viol.	✓ Clean	`C[C@@]1(O)c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C…`
ZINC71769638 ZINC	0.793	416.4 Da LogP -0.82 TPSA 204.4	1 viol.	✓ Clean	`C[C@@]1(O)c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C…`
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`
ZINC12501413 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC12958448 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC1532555 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC16546189 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC2159505 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3073318 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869963 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869965 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC9334496 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](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`
ZINC22054932 ZINC	0.762	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3C…`
ZINC44019569 ZINC	0.762	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C(…`

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.