KpKP13 Protein target profile

transketolase 2

Accession: KP13_32378

Gene: AHE43322.1 tkt2 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GW02

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Length 664

Pocket druggability (P2Rank · AlphaFold DB model) 0.9

Direct ligand evidence 0 74 total records

Functional annotation 1 EC 5 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: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.90, FPocket 0.81). 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 0.81. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.90. 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 (%): 35.915 Lower values reduce human off-target concern.
Human E-value: 1.23e-16
Gut microbiome similarity: 8.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 77.61 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 98.17 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.9

Structure A0A0H3GW02

Pocket Pocket 1

Druggability (FPocket) 0.807

Structure A0A0H3GW02

Pocket Pocket 2

ColabFold model

P2Rank 0.839 · Pocket 1

FPocket 0.391 · Pocket 13

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 411 / 4744 genomes with a hit

Prevalence 8.7%

Sequence

Primary amino-acid sequence viewer.

MSRRELANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWNDFLKHNPQNPDWVDRDRFILSNGHASMLLYSLLHLTGYDLPLSELKQFRQLHSKTPGHPEHGYTPGVETTTGPLGQGLANAVGMAIAERTLVAQFNRPGHEIIDHHTWVFMGDGCLMEGISHEACSLAGTLGLGKLIGFYDHNGISIDGKTEGWFSDDTAERFRAYHWHVIGDIDGHDPQAIKQAITEAQAVKDKPSLIICRTIIGFGSPNKAGSEESHGAALGEKEVALARQQLGWKYPPFEIPKEIYAGWDARPRGEKAEHAWNEKFAAYQQQFPELAAELTRRMNGALPEDFAATARDYVAKLQAEPAKIASRKASQNALNAYGPHLPELLGGSADLAPSNLTIWSGSTSIKEDPAGNYIHYGVREFGMTAVANGIALHGGFIPYTSTFLMFVEYARNAARMAALMKARQIMVYTHDSIGLGEDGPTHQAVEQLASLRLTPNFSTWRPCDQVETAVAWQAAIARQGGPTALILSRQNLAQMPRTPEQVQDIARGGYVLKDAGGKPDLILIATGSEVEITVLAAEKLLAKGVNVRVVSLPSTDVFDAQDEAWRESVLPSDVSARVAVEAGIADYWYKYVGLKGKIVGMTGYGESAPAEQLFPFFGFTVDHIVATAEQVLNG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.2.1.1

Gene Ontology (GO)

GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0004802 Catalysis of the reversible transfer of a 2-carbon ketol group (CH2OH-CO-) from a ketose phosphate donor to an aldose phosphate acceptor.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046872 Binding to a metal ion.
GO:0009052 The branch of the pentose-phosphate shunt which does not involve oxidation reactions. It comprises a series of sugar phosphate interconversions, starting with ribulose 5-P and producing fructose 6-P and glyceraldehyde 3-P.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
5	663	NCBIfam	TIGR00232	transketolase
5	663	InterPro	IPR005478	Transketolase, bacterial-like
466	482	ProSitePatterns	PS00802	Transketolase signature 2.
466	482	InterPro	IPR020826	Transketolase binding site
353	523	Pfam	PF02779	Transketolase, pyrimidine binding domain
353	523	InterPro	IPR005475	Transketolase-like, pyrimidine-binding domain
333	525	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
333	525	InterPro	IPR029061	Thiamin diphosphate-binding fold
541	654	Pfam	PF02780	Transketolase, C-terminal domain
541	654	InterPro	IPR033248	Transketolase, C-terminal domain
532	663	SUPERFAMILY	SSF52922	TK C-terminal domain-like
532	663	InterPro	IPR009014	Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II
326	536	Gene3D	G3DSA:3.40.50.970	-
354	524	SMART	SM00861	Transket_pyr_3
354	524	InterPro	IPR005475	Transketolase-like, pyrimidine-binding domain
4	320	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
4	320	InterPro	IPR029061	Thiamin diphosphate-binding fold
326	536	FunFam	G3DSA:3.40.50.970:FF:000003	Transketolase
1	325	FunFam	G3DSA:3.40.50.970:FF:000004	Transketolase
358	519	CDD	cd07033	TPP_PYR_DXS_TK_like
11	31	ProSitePatterns	PS00801	Transketolase signature 1.
11	31	InterPro	IPR005474	Transketolase, N-terminal
2	325	Gene3D	G3DSA:3.40.50.970	-
8	273	CDD	cd02012	TPP_TK
8	273	InterPro	IPR005474	Transketolase, N-terminal
537	663	Gene3D	G3DSA:3.40.50.920	-
537	663	InterPro	IPR009014	Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II
2	662	PANTHER	PTHR43522	TRANSKETOLASE
2	662	InterPro	IPR033247	Transketolase family
537	663	FunFam	G3DSA:3.40.50.920:FF:000003	Transketolase
3	333	Pfam	PF00456	Transketolase, thiamine diphosphate binding domain
3	333	InterPro	IPR005474	Transketolase, N-terminal

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.9

Likely same site as FPocket 1 1.8 Å 19 shared residues 95% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.192

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Surrounding area

Pocket 3 P2Rank #3

0.161

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Surrounding area

Pocket 4 P2Rank #4

0.085

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Surrounding area

Pocket 5 P2Rank #5

0.05

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #2

0.807 Unusual size

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Surrounding area

Pocket 2 FPocket #1

0.47

Likely same site as P2Rank 1 1.8 Å 19 shared residues 95% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:410-410 Proton donor

UniProt: Binding site:113-115

UniProt: Binding site:154-154

UniProt: Binding site:155-155

UniProt: Binding site:184-184

UniProt: Binding site:186-186

UniProt: Binding site:25-25

UniProt: Binding site:260-260

UniProt: Binding site:357-357

UniProt: Binding site:384-384

UniProt: Binding site:436-436

UniProt: Binding site:460-460

UniProt: Binding site:468-468

UniProt: Binding site:472-472

UniProt: Binding site:519-519

UniProt: Binding site:65-65

UniProt: Site:25-25 Important for catalytic activity

UniProt: Site:260-260 Important for catalytic activity

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.839

Likely same site as FPocket 2 1.8 Å 16 shared residues 84% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.191

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Surrounding area

Pocket 3 P2Rank #3

0.121

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Surrounding area

Pocket 4 P2Rank #4

0.082

Likely same site as FPocket 13 2.3 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.077

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #13

0.391

Likely same site as P2Rank 4 2.3 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #16

0.298

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Surrounding area

Pocket 3 FPocket #2

0.264 Unusual size

Likely same site as P2Rank 1 1.8 Å 16 shared residues 84% of smaller site

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Surrounding area

Pocket 4 FPocket #4

0.2 Unusual size

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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_A0A0H3GW02	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_32378	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.

74 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 24 records from similar proteins

Structural ligands 24 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5SP PDB via homolog 230.1 Da · LogP -2.62 · TPSA 144.5 Open detail RCSB PDB

8EF PDB via homolog Detail RCSB PDB

8EL PDB via homolog Detail RCSB PDB

8EO PDB via homolog Detail RCSB PDB

8FL 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
5SP RCSB PDB	5I5E	P34736	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`C([C@H]([C@@H](C(=O)CO)O)O)OP(=O)(O)O`
8EF RCSB PDB	5XTV	P34736	426.3 Da LogP 1.37 TPSA 168.3	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN2CS[C@H](C2=C)CCOP(=O)(O)OP(=O)…`
8EL RCSB PDB	5XSA	P34736	426.3 Da LogP 1.72 TPSA 168.3	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN2CSC(=C2C)CCOP(=O)(O)OP(=O)(O)O`
8EO RCSB PDB	5XSM	P34736	427.3 Da LogP 1.03 TPSA 168.1	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)C[N+]2=C([C@@H](SC2)CCOP(=O)(O)OP…`
8FL RCSB PDB	5XUF	P34736	442.3 Da LogP 1.04 TPSA 188.6	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN2[C@@H](SC(=C2C)CCOP(=O)(O)OP(=…`
8GF RCSB PDB	5XTL	P34736	109.1 Da LogP 0.37 TPSA 51.8	✓ Ro5	✓ Clean	`Cc1nccc(n1)N`
8ML RCSB PDB	5XTX	P34736	686.5 Da LogP -2.34 TPSA 336.2	3 viol.	✓ Clean	`Cc1ncc(c(n1)N)CN2C(SC(C2=C)CCOP(=O)(O)OP(=O)(O)…`
8N9 RCSB PDB	5XU9	P34736	484.4 Da LogP 1.48 TPSA 208.8	2 viol.	✓ Clean	`Cc1ncc(c(n1)N)CN\2C(=C(S/C2=C(\CO)/O)CCOP(=O)(O…`
BTB RCSB PDB	3M49	A0A6L7H165	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
E4P RCSB PDB	5XPS	P34736	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`C([C@H]([C@H](C=O)O)O)OP(=O)(O)O`
F6R RCSB PDB	5I51	P34736	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H](C(=O)CO)O)O)O)OP(=O)(O)O`
HSX RCSB PDB	5XQA	P34736	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@H](O1)O)O)O)OP(=O)(O)O`
I22 RCSB PDB	5HJE	P34736	290.2 Da LogP -3.90 TPSA 185.0	1 viol.	✓ Clean	`C([C@H]([C@H]([C@H]([C@@H](C(=O)CO)O)O)O)O)OP(=…`
M6T RCSB PDB	1TKC	P23254	438.3 Da LogP 0.52 TPSA 171.8	✓ Ro5	✓ Clean	`Cc1c(c(nc(n1)C)N)C[n+]2csc(c2C)CCO[P@](=O)(O)O[…`
N1T RCSB PDB	1TKB	P23254	423.3 Da LogP 0.81 TPSA 158.9	✓ Ro5	✓ Clean	`Cc1ccc(c(n1)N)C[n+]2csc(c2C)CCO[P@](=O)(O)O[P@@…`
N3T RCSB PDB	1TKA	P23254	423.3 Da LogP 0.81 TPSA 158.9	✓ Ro5	✓ Clean	`Cc1cc(c(cn1)C[n+]2csc(c2C)CCO[P@](=O)(O)O[P@@](…`
NDQ RCSB PDB	6TJ8	P27302	441.3 Da LogP 0.54 TPSA 178.2	✓ Ro5	✓ Clean	`Cc1c(sc[n+]1Cc2cnc(nc2N)OC)CCOP(=O)(O)OP(=O)(O)O`
P23 RCSB PDB	5XTL	P34736	220.1 Da LogP 0.62 TPSA 113.3	✓ Ro5	✓ Clean	`CCCO[P@@](=O)(O)OP(=O)(O)O`
PG5 RCSB PDB	3M49	A0A6L7H165	178.2 Da LogP 0.31 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOC`
POP RCSB PDB	5I5G	P34736	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
R5P RCSB PDB	3M6L	Q0P7Y3	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`C(C(C(C(C=O)O)O)O)OP(=O)(O)O`
RP5 RCSB PDB	3M7I	Q0P7Y3	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@@H](O1)O)O)O)OP(=O)(O)O`
T5X RCSB PDB	5XQK	P34736	655.4 Da LogP -2.15 TPSA 316.6	3 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@](CO)([C@H]([C@@H…`
T6F RCSB PDB	5XT0	P34736	685.5 Da LogP -2.79 TPSA 336.9	3 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@](CO)([C@H]([C@@H…`

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
ZINC12504154 ZINC	1.000	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H]1O`
ZINC1530556 ZINC	1.000	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532546 ZINC	1.000	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H]1O`
ZINC1615342 ZINC	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC1692489 ZINC	1.000	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC22116391 ZINC	1.000	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC3606137 ZINC	1.000	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC3869426 ZINC	1.000	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC4096190 ZINC	1.000	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H]1O`
ZINC4228241 ZINC	1.000	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H]1O`
ZINC4521831 ZINC	1.000	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H]1O`
ZINC4530388 ZINC	1.000	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5701172 ZINC	1.000	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861 ZINC	1.000	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC8551307 ZINC	1.000	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC8551308 ZINC	1.000	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC100351935 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@…`
ZINC1529564 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@…`
ZINC1532533 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC1532857 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…`
ZINC3581460 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…`
ZINC38276879 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC38276880 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@H…`
ZINC3869397 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C…`
ZINC3875374 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC3875375 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@…`
ZINC4095545 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC4095546 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H…`
ZINC4096188 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H](O)[C@…`
ZINC8551507 ZINC	0.962	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC100033330 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC100067275 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC100889630 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC104861723 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O…`
ZINC12503760 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC12503763 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC19850142 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC2508229 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC4545927 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)COP(=O)(…`
ZINC4545928 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)COP(=O)(O…`
ZINC4545929 ZINC	0.889	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)COP(=O)(O…`
ZINC1532601 ZINC	0.778	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC32786787 ZINC	0.778	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC13516910 ZINC	0.759	244.1 Da LogP -2.42 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC2562340 ZINC	0.759	244.1 Da LogP -2.42 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC4097102 ZINC	0.742	259.2 Da LogP -3.14 TPSA 162.7	1 viol.	✓ Clean	`N[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC4097103 ZINC	0.742	259.2 Da LogP -3.14 TPSA 162.7	1 viol.	✓ Clean	`N[C@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC34764844 ZINC	0.733	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC71254558 ZINC	0.688	444.6 Da LogP 0.70 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCS`

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.

Cross-references

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

Sequence

UniProt A0A0H3GW02