KpKP13 Protein target profile

putative transketolase family protein

Accession: KP13_04322

Gene: AHE45556.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A086ID01

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Length 330

Pocket druggability (P2Rank · AlphaFold DB model) 0.033

Direct ligand evidence 0 93 total records

Functional annotation 1 EC 2 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.

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 (%): 35.294 Lower values reduce human off-target concern.
Human E-value: 9.4e-24
Gut microbiome similarity: 0.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 94.64 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) 0.033

Structure A0A086ID01

Pocket Pocket 1

Druggability (FPocket) 0.132

Structure A0A086ID01

Pocket Pocket 5

ColabFold model

P2Rank 0.195 · Pocket 1

FPocket 0.909 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 31 / 4744 genomes with a hit

Prevalence 0.7%

Cross-references

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

Sequence

UniProt A0A086ID01

Chemistry

ChEMBL CHEMBL403691 ChEMBL CHEMBL255603 ChEMBL CHEMBL271044 ChEMBL CHEMBL256627 ChEMBL CHEMBL270613 ChEMBL CHEMBL401948 ChEMBL 0YN ChEMBL TZD ChEMBL CHEMBL252086 ChEMBL CHEMBL403212 ChEMBL CHEMBL401817 ChEMBL CHEMBL256831 ChEMBL CHEMBL402329 ChEMBL CHEMBL402566 ChEMBL CHEMBL255340 ChEMBL CHEMBL252441 ChEMBL CHEMBL258077 ChEMBL CHEMBL256454 ChEMBL CHEMBL255339 ChEMBL CHEMBL270632 ChEMBL CHEMBL403365 ChEMBL CHEMBL255541 ChEMBL CHEMBL255542 ChEMBL CHEMBL429246 ChEMBL CHEMBL271521 ChEMBL CHEMBL270168 ChEMBL CHEMBL252637 ChEMBL CHEMBL270384 ChEMBL CHEMBL2104121 ChEMBL CHEMBL430409

Sequence

Primary amino-acid sequence viewer.

MSQSQPRLKTSAMIASIADEGQATVPAPFGVALSKLAAQRPEIVGMTADLSKYTDLHIFAQAFPDRFFQMGMAEQLLMAAAGGMAKEGFIPFATTYAAFATRRAYDFIHQVIAEEHLNVKICAALPGLTTGYGPSHQATEDLAIMRGIPGMVIVDPCDALEIEQAVPAIADHQGPVYMRLLRGKVPLVLDKYDYQFELGKAKLLEDGNDVLIISSGLMTMRALEAAEKLRADNIGVAVLHVPTIKPLDEKAIIEQASKPGRLVVTAENHTAVGGLGEAVAALLMRKGVRCELDSVGLPDAFLLAGALPTLHDRYGISTAKIVEKIKYRLR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 2 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.2.1.7

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:0008661 Catalysis of the reaction: D-glyceraldehyde 3-phosphate + H+ + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
199	321	Pfam	PF02780	Transketolase, C-terminal domain
199	321	InterPro	IPR033248	Transketolase, C-terminal domain
4	329	PANTHER	PTHR43825	PYRUVATE DEHYDROGENASE E1 COMPONENT
29	182	CDD	cd07033	TPP_PYR_DXS_TK_like
23	187	SMART	SM00861	Transket_pyr_3
23	187	InterPro	IPR005475	Transketolase-like, pyrimidine-binding domain
4	187	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
4	187	InterPro	IPR029061	Thiamin diphosphate-binding fold
8	198	Gene3D	G3DSA:3.40.50.970	-
199	328	Gene3D	G3DSA:3.40.50.920	-
199	328	InterPro	IPR009014	Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II
29	185	Pfam	PF02779	Transketolase, pyrimidine binding domain
29	185	InterPro	IPR005475	Transketolase-like, pyrimidine-binding domain
20	198	FunFam	G3DSA:3.40.50.970:FF:000129	Transketolase
193	329	SUPERFAMILY	SSF52922	TK C-terminal domain-like
193	329	InterPro	IPR009014	Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II

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

0.033

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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 #1

0.909 Unusual size

Likely same site as P2Rank 2 7.3 Å 6 shared residues 60% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #2

0.226

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_A0A086ID01	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04322	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.

93 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 43 records from similar proteins

Structural ligands 13 0 loaded crystals

Measured bioactivity 30 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1U0 PDB via homolog 483.4 Da · LogP 1.12 · TPSA 205.5 Open detail RCSB PDB

1Y7 PDB via homolog Detail RCSB PDB

4MV PDB via homolog Detail RCSB PDB

DX5 PDB via homolog Detail RCSB PDB

E4P 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
1U0 RCSB PDB	4KXY	P29401	483.4 Da LogP 1.12 TPSA 205.5	1 viol.	✓ Clean	`Cc1c(sc(c1Cc2cnc(nc2N)C)[C@@H](CO)O)CCOP(=O)(O)…`
1Y7 RCSB PDB	4KXX	P29401	292.2 Da LogP -4.11 TPSA 188.1	1 viol.	✓ Clean	`C([C@@H]([C@H]([C@@H]([C@@H]([C@@H](COP(=O)(O)O…`
4MV RCSB PDB	1UMC	Q5SLR3	116.2 Da LogP 1.51 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC(=O)O`
DX5 RCSB PDB	4KXW	P29401	232.1 Da LogP -2.83 TPSA 147.7	1 viol.	✓ Clean	`C([C@@H]([C@H]([C@@H](COP(=O)(O)O)O)O)O)O`
E4P RCSB PDB	1NGS	P23254	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`C([C@H]([C@H](C=O)O)O)OP(=O)(O)O`
HTL RCSB PDB	6OUW	Q9RUB5	467.4 Da LogP 1.04 TPSA 186.0	✓ Ro5	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)C(=O)C)CCO[P@@](=O)(…`
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@@](…`
PYR RCSB PDB	3DV0	P21874	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
S6P RCSB PDB	4KXU	P29401	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`C([C@@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)…`
T6F RCSB PDB	6HA3	P29401	685.5 Da LogP -2.79 TPSA 336.9	3 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@](CO)([C@H]([C@@H…`
TDK RCSB PDB	6OUV	Q9RUB5	563.4 Da LogP 0.84 TPSA 235.7	3 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@@](C)(O)[P@@](=O)…`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL403691 ChEMBL	P29401	8.33 ~4.7 nM	306.4 Da LogP 1.78 TPSA 69.1	✓ Ro5	✓ Clean	`CC(=O)OCCc1sc[n+](Cc2ccc(C)nc2N)c1C`
CHEMBL255603 ChEMBL	P29401	8.15 ~7.1 nM	250.3 Da LogP 0.90 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1c(CCO)sc[n+]1Cc1ccc(N)nc1`
CHEMBL271044 ChEMBL	P29401	8.08 ~8.3 nM	278.4 Da LogP 1.52 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1cc(C)c(C[n+]2csc(CCO)c2C)c(N)n1`
CHEMBL256627 ChEMBL	P29401	8.06 ~8.7 nM	278.4 Da LogP 1.47 TPSA 63.0	✓ Ro5	✓ Clean	`CCc1ccc(C[n+]2csc(CCO)c2C)c(N)n1`
CHEMBL270613 ChEMBL	P29401	8.05 ~8.9 nM	284.8 Da LogP 1.56 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1c(CCO)sc[n+]1Cc1ccc(Cl)nc1N`
CHEMBL401948 ChEMBL	P29401	8.05 ~8.9 nM	320.2 Da LogP -1.44 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1c(CCO)sc[n+]1Cc1ccc(Cl)nc1N.[Cl-]`
0YN ChEMBL	P29401	7.92 ~12.0 nM	263.4 Da LogP 1.86 TPSA 72.0	✓ Ro5	✓ Clean	`Cc1c(csc1CCO)Cc2cnc(nc2N)C`
TZD ChEMBL	P29401	7.80 ~15.8 nM	440.3 Da LogP 0.72 TPSA 187.1	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN2C(=C(SC2=O)CCO[P@@](=O)(O)OP(=…`
CHEMBL252086 ChEMBL	P29401	7.75 ~17.8 nM	299.8 Da LogP -1.78 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2csc(CCO)c2C)c(N)n1.[Cl-]`
CHEMBL403212 ChEMBL	P29401	7.68 ~20.9 nM	292.4 Da LogP 1.78 TPSA 63.0	✓ Ro5	✓ Clean	`CCc1sc(CCO)c(C)[n+]1Cc1ccc(C)nc1N`
CHEMBL401817 ChEMBL	P29401	7.66 ~21.9 nM	424.3 Da LogP 1.45 TPSA 156.1	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2csc(CCOP(=O)(O)OP(=O)(O)O)c2C)c(N)…`
CHEMBL256831 ChEMBL	P29401	7.64 ~22.9 nM	307.4 Da LogP 0.86 TPSA 92.1	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(C[n+]2csc(CCO)c2C)c(N)n1`
CHEMBL402329 ChEMBL	P29401	7.60 ~25.1 nM	278.4 Da LogP 1.52 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2c(C)sc(CCO)c2C)c(N)n1`
CHEMBL402566 ChEMBL	P29401	7.60 ~25.1 nM	280.4 Da LogP 0.40 TPSA 83.2	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2csc(CCO)c2CO)c(N)n1`
CHEMBL255340 ChEMBL	P29401	7.57 ~26.9 nM	280.4 Da LogP 0.70 TPSA 83.2	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2csc([C@@H](O)CO)c2C)c(N)n1`
CHEMBL252441 ChEMBL	P29401	7.55 ~28.2 nM	313.9 Da LogP -1.47 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2c(C)sc(CCO)c2C)c(N)n1.[Cl-]`
CHEMBL258077 ChEMBL	P29401	7.55 ~28.2 nM	280.4 Da LogP 0.70 TPSA 83.2	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2csc([C@H](O)CO)c2C)c(N)n1`
CHEMBL256454 ChEMBL	P29401	7.54 ~28.8 nM	250.3 Da LogP 0.90 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2csc(CCO)c2)c(N)n1`
CHEMBL255339 ChEMBL	P29401	7.52 ~30.2 nM	308.4 Da LogP 1.27 TPSA 83.2	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2c(C(C)O)sc(CCO)c2C)c(N)n1`
CHEMBL270632 ChEMBL	P29401	7.44 ~36.3 nM	264.4 Da LogP 1.21 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2cc(CCO)sc2C)c(N)n1`
CHEMBL403365 ChEMBL	P29401	7.44 ~36.3 nM	250.3 Da LogP 0.90 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1c(CCO)sc[n+]1Cc1cccnc1N`
CHEMBL255541 ChEMBL	P29401	7.40 ~39.8 nM	278.4 Da LogP 1.47 TPSA 63.0	✓ Ro5	✓ Clean	`CCc1c(CCO)sc[n+]1Cc1ccc(C)nc1N`
CHEMBL255542 ChEMBL	P29401	7.28 ~52.5 nM	280.4 Da LogP 0.70 TPSA 83.2	✓ Ro5	✓ Clean	`Cc1ccc(C[n+]2csc(C(O)CO)c2C)c(N)n1`
CHEMBL429246 ChEMBL	P29401	7.24 ~57.5 nM	275.4 Da LogP 0.78 TPSA 86.8	✓ Ro5	✓ Clean	`Cc1c(CCO)sc[n+]1Cc1ccc(C#N)nc1N`
CHEMBL271521 ChEMBL	P29401	7.19 ~64.6 nM	250.3 Da LogP 0.90 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1c(CCO)sc[n+]1Cc1cnccc1N`
CHEMBL270168 ChEMBL	P29401	6.98 ~104.7 nM	318.3 Da LogP 1.92 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1c(CCO)sc[n+]1Cc1ccc(C(F)(F)F)nc1N`
CHEMBL252637 ChEMBL	P29401	6.96 ~109.6 nM	285.8 Da LogP -2.09 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1c(CCO)sc[n+]1Cc1cccnc1N.[Cl-]`
CHEMBL270384 ChEMBL	P29401	6.96 ~109.6 nM	376.2 Da LogP 1.51 TPSA 63.0	✓ Ro5	✓ Clean	`Cc1c(CCO)sc[n+]1Cc1cc(I)cnc1N`
CHEMBL2104121 ChEMBL	Q9RUB5	6.94 ~114.8 nM	460.8 Da LogP -2.15 TPSA 169.0	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCOP(=O)(O)OP(=O)(O)O)c2C)c(N)…`
CHEMBL430409 ChEMBL	P29401	6.77 ~169.8 nM	423.3 Da LogP 1.56 TPSA 148.7	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCOP(C)(=O)OP(=O)(O)O)c2C)c(N)…`

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
ZINC1532601 ZINC	1.000	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	1.000	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC8215517 ZINC	0.981	425.3 Da LogP 0.84 TPSA 169.0	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCO[P@@](=O)(O)OP(=O)(O)O)c2C)…`
ZINC1532839 ZINC	0.852	345.3 Da LogP 0.72 TPSA 122.4	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCOP(=O)(O)O)c2C)c(N)n1`
ZINC13520374 ZINC	0.807	426.3 Da LogP 0.97 TPSA 163.2	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCO[P@@](=O)(O)OP(=O)(O)O)c2C)…`
ZINC1530556 ZINC	0.778	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`
ZINC22116391 ZINC	0.778	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	0.778	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	0.778	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`
ZINC8551307 ZINC	0.778	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	0.778	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`
ZINC100033330 ZINC	0.750	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	0.750	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	0.750	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	0.750	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	0.750	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	0.750	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	0.750	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	0.750	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	0.750	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	0.750	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	0.750	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…`
ZINC5159740 ZINC	0.690	307.4 Da LogP 1.18 TPSA 82.0	✓ Ro5	✓ Clean	`CC(=O)OCCc1sc[n+](Cc2cnc(C)nc2N)c1C`
ZINC1569986051 ZINC	0.672	324.5 Da LogP 1.50 TPSA 88.8	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCOC(=N)S)c2C)c(N)n1`
ZINC65748831 ZINC	0.667	345.4 Da LogP 0.43 TPSA 119.3	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCOS(=O)(=O)O)c2C)c(N)n1`
ZINC49153 ZINC	0.643	265.4 Da LogP 0.61 TPSA 75.9	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCO)c2C)c(N)n1`
ZINC1841074 ZINC	0.636	200.3 Da LogP 3.85 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCC(=O)O`
ZINC2013445 ZINC	0.636	214.3 Da LogP 4.24 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCCC(=O)O`
ZINC2575042 ZINC	0.636	228.4 Da LogP 4.63 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCCCC(=O)O`
ZINC167956596 ZINC	0.625	281.4 Da LogP 1.55 TPSA 55.7	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCS)c2C)c(N)n1`
ZINC3209500 ZINC	0.625	369.5 Da LogP 2.47 TPSA 82.0	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCOC(=O)c3ccccc3)c2C)c(N)n1`
ZINC2522549 ZINC	0.621	214.1 Da LogP -1.59 TPSA 124.3	✓ Ro5	✓ Clean	`O=CC[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC4543673 ZINC	0.621	214.1 Da LogP -1.59 TPSA 124.3	✓ Ro5	✓ Clean	`O=CC[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC4543675 ZINC	0.621	214.1 Da LogP -1.59 TPSA 124.3	✓ Ro5	✓ Clean	`O=CC[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC4543677 ZINC	0.621	214.1 Da LogP -1.59 TPSA 124.3	✓ Ro5	✓ Clean	`O=CC[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC100657408 ZINC	0.613	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC215934438 ZINC	0.613	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC255961849 ZINC	0.613	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC255961850 ZINC	0.613	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC5132021 ZINC	0.613	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC13540298 ZINC	0.591	440.3 Da LogP 0.72 TPSA 187.1	✓ Ro5	✓ Clean	`Cc1ncc(Cn2c(C)c(CCO[P@@](=O)(O)OP(=O)(O)O)sc2=O…`
ZINC1497913 ZINC	0.588	427.6 Da LogP 3.23 TPSA 82.0	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCOC(=O)C3C4CC5CC(C4)CC3C5)c2C…`
ZINC8398853 ZINC	0.588	441.6 Da LogP 3.77 TPSA 82.0	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCOC(=O)CC34CC5CC(CC(C5)C3)C4)…`
ZINC145838685 ZINC	0.583	200.3 Da LogP 3.70 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC[C@@H](C)CCCC(=O)O`
ZINC145838882 ZINC	0.583	200.3 Da LogP 3.70 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC[C@H](C)CCCC(=O)O`
ZINC25721582 ZINC	0.581	244.1 Da LogP -2.23 TPSA 144.5	✓ Ro5	✓ Clean	`O=CC[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC25721586 ZINC	0.581	244.1 Da LogP -2.23 TPSA 144.5	✓ Ro5	✓ Clean	`O=CC[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC4544030 ZINC	0.581	244.1 Da LogP -2.23 TPSA 144.5	✓ Ro5	✓ Clean	`O=CC[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC4544032 ZINC	0.581	244.1 Da LogP -2.23 TPSA 144.5	✓ Ro5	✓ Clean	`O=CC[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC4544034 ZINC	0.581	244.1 Da LogP -2.23 TPSA 144.5	✓ Ro5	✓ Clean	`O=CC[C@H](O)[C@@H](O)[C@H](O)COP(=O)(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.

putative transketolase family protein

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

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Cross-references

Sequence

Chemistry

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence