Protein profile

KP13_32378

transketolase 2

Genome: KpKP13

Gene: AHE43322.1 tkt2 Structure source: AlphaFold + ColabFold UniProt A0A0H3GW02

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Amino acids 664

Annotations 6

Features 32

PDB binders 24

Druggability 0.807

Overview

Basic information about this protein and its source genome.

Accession: KP13_32378
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43322.1 tkt2
Status: annotated
Amino acids: 664
Structure source: AlphaFold + ColabFold

2.2.1.1

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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 35.915
Human E-value: 1.23e-16
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 77.61
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 98.17

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.807

Structure A0A0H3GW02

Pocket Pocket 2

P2Rank 0.9

Structure A0A0H3GW02

Pocket Pocket 1

ColabFold model

FPocket 0.391 · Pocket 13

P2Rank 0.839 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 411 / 4744 genomes with a hit

Normalized 0.087

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

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 Features

Domain/signature hits 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; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GW02	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_32378	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
2				0.807
1				0.47

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	14.99	0.741
2	3.51	0.128
3	2.95	0.095
4	2.23	0.055
5	1.24	0.012

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
13				0.391
16				0.298
2				0.264

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	10.78	0.578
2	3.81	0.148
3	2.19	0.052
4	2.11	0.048
5	1.09	0.007

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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	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	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	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	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	5XTL	P34736	109.1 Da LogP 0.37 TPSA 51.8	✓ Ro5	✓ Clean	`Cc1nccc(n1)N`
8ML	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	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	3M49	A0A6L7H165	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
E4P	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	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	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	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	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	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	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	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	5XTL	P34736	220.1 Da LogP 0.62 TPSA 113.3	✓ Ro5	✓ Clean	`CCCO[P@@](=O)(O)OP(=O)(O)O`
PG5	3M49	A0A6L7H165	178.2 Da LogP 0.31 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOC`
POP	5I5G	P34736	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
R5P	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	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	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	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	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	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	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	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC1692489	1.000	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC22116391	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	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	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	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	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	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	1.000	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5701172	1.000	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861	1.000	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC8551307	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	0.733	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
ZINC34317654	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC71254558	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.