Protein profile

KP13_02546

putative thiamin pyrophosphate enzyme

Genome: KpKP13

Gene: AHE43009.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GUE2

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Amino acids 569

Annotations 8

Features 24

PDB binders 34

Druggability 0.852

Overview

Basic information about this protein and its source genome.

Accession: KP13_02546
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43009.1
Status: annotated
Amino acids: 569
Structure source: AlphaFold + ColabFold

GO:0030976 Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases. 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:0000287 Binding to a magnesium (Mg) ion. GO:0005948 A dimeric (a large and a small chain) or tetrameric (two large and two small chains) enzyme complex. Catalyzes the formation of acetolactate from pyruvate. GO:0003984 Catalysis of the reaction: H+ + 2 pyruvate = (2S)-2-acetolactate + CO2. Can also convert 2-oxobutanoate and pyruvate to (S)-2-ethyl-2-hydroxy-3-oxobutanoate. GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 95.69

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 0.852

Structure A0A0H3GUE2

Pocket Pocket 26

P2Rank 0.614

Structure A0A0H3GUE2

Pocket Pocket 1

ColabFold model

FPocket 0.556 · Pocket 12

P2Rank 0.514 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 6 / 4744 genomes with a hit

Normalized 0.001

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

GO:0030976 Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
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:0000287 Binding to a magnesium (Mg) ion.
GO:0005948 A dimeric (a large and a small chain) or tetrameric (two large and two small chains) enzyme complex. Catalyzes the formation of acetolactate from pyruvate.
GO:0003984 Catalysis of the reaction: H+ + 2 pyruvate = (2S)-2-acetolactate + CO2. Can also convert 2-oxobutanoate and pyruvate to (S)-2-ethyl-2-hydroxy-3-oxobutanoate.
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0009097 OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
GO:0009099 The chemical reactions and pathways resulting in the formation of valine, 2-amino-3-methylbutanoic acid.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
19	569	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
379	569	Gene3D	G3DSA:3.40.50.970	-
415	567	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
415	567	InterPro	IPR029061	Thiamin diphosphate-binding fold
6	567	PANTHER	PTHR18968	THIAMINE PYROPHOSPHATE ENZYMES
6	567	InterPro	IPR045229	Thiamine pyrophosphate enzyme
3	196	Gene3D	G3DSA:3.40.50.970	-
1	18	Phobius	SIGNAL_PEPTIDE	Signal peptide region
414	565	Pfam	PF02775	Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
414	565	InterPro	IPR011766	Thiamine pyrophosphate enzyme, TPP-binding
2	13	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
172	359	SUPERFAMILY	SSF52467	DHS-like NAD/FAD-binding domain
172	359	InterPro	IPR029035	DHS-like NAD/FAD-binding domain superfamily
14	18	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
211	314	Pfam	PF00205	Thiamine pyrophosphate enzyme, central domain
211	314	InterPro	IPR012000	Thiamine pyrophosphate enzyme, central domain
207	378	Gene3D	G3DSA:3.40.50.1220	-
1	1	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
1	18	SignalP_EUK	SignalP-noTM	SignalP-noTM
7	186	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
7	186	InterPro	IPR029061	Thiamin diphosphate-binding fold
7	187	Pfam	PF02776	Thiamine pyrophosphate enzyme, N-terminal TPP binding domain
7	187	InterPro	IPR012001	Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
10	179	CDD	cd07035	TPP_PYR_POX_like

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_A0A0H3GUE2	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02546	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
26				0.852
1				0.823
2				0.514

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	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				7.82	0.415
2				2.87	0.091

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
12				0.556
8				0.445
27				0.276

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	7.37	0.385
2	4.19	0.17
3	1.72	0.03
4	1.36	0.016

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.

89 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
1MM	1T9D	P07342	381.4 Da LogP 0.49 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1nc(nc(n1)OC)NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC`
1PG	4D5E	P0CH62	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
1SM	6DEP	A0A1D8PJF9	364.4 Da LogP 1.39 TPSA 127.3	✓ Ro5	✓ Clean	`Cc1cc(nc(n1)NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)C`
60G	6DEM	A0A1D8PJF9	410.4 Da LogP 0.93 TPSA 145.8	✓ Ro5	✓ Clean	`COc1cc(nc(n1)NC(=O)NS(=O)(=O)Cc2ccccc2C(=O)OC)OC`
6R4	6DES	A0A1D8PJF9	398.4 Da LogP 0.10 TPSA 138.6	✓ Ro5	✓ Clean	`CCCOC1=NN(C(=O)N1C)C(=O)NS(=O)(=O)c2ccccc2C(=O)…`
8GF	6WO1	Q96VZ6	109.1 Da LogP 0.37 TPSA 51.8	✓ Ro5	✓ Clean	`Cc1nccc(n1)N`
8PA	3F6B	P20906	558.5 Da LogP 1.98 TPSA 202.1	1 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@H](\C=C\c3cccnc3)…`
AUJ	5WKC	P07342	—	—	—	`Cc1ncc(c(n1)N)C[N]2=C(SC(=C2C)CCOP(=O)(O)OP(=O)…`
AYD	1N0H	P07342	382.3 Da LogP 0.98 TPSA 177.1	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN/C(=C/CCO[P@@](=O)(O)OP(=O)(O)O…`
CIE	1N0H	P07342	414.8 Da LogP 1.83 TPSA 136.6	✓ Ro5	✓ Clean	`CCOC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc2nc(cc(n2)Cl)OC`
CO2	6BD3	P07342	44.0 Da LogP -0.58 TPSA 34.1	✓ Ro5	✓ Clean	`C(=O)=O`
CXO	2PGN	P0CH62	112.1 Da LogP 0.70 TPSA 34.1	✓ Ro5	Alert	`C1CCC(=O)C(=O)C1`
D7K	3FSJ	P20906	625.5 Da LogP 1.87 TPSA 235.7	3 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@@](c3ccccc3)(O)[P…`
DPO	6WO1	Q96VZ6	173.9 Da LogP -3.34 TPSA 135.6	✓ Ro5	✓ Clean	`[O-]P(=O)([O-])OP(=O)([O-])[O-]`
DTT	1N0H	P07342	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
F50	5WKC	P07342	76.1 Da LogP 0.02 TPSA 46.5	✓ Ro5	✓ Clean	`CC(=O)OO`
G87	6DER	A0A1D8PJF9	418.3 Da LogP 2.56 TPSA 107.7	✓ Ro5	✓ Clean	`Cc1ccc(c(c1Cl)NS(=O)(=O)c2nc3nc(cc(n3n2)OC)OC)Cl`
G8A	6DEN	A0A1D8PJF9	506.3 Da LogP 1.78 TPSA 136.6	1 viol.	✓ Clean	`CCOC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc2nc(cc(n2)I)OC`
G8G	6DEL	A0A1D8PJF9	442.3 Da LogP 1.10 TPSA 185.4	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN(C=O)/C(=C(/CCOP(=O)(O)OP(=O)(O…`
H4V	6DEO	A0A1D8PJF9	492.3 Da LogP 1.39 TPSA 136.6	✓ Ro5	✓ Clean	`COc1cc(nc(n1)NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)I`
HTL	6BD3	P07342	467.4 Da LogP 1.04 TPSA 186.0	✓ Ro5	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)C(=O)C)CCO[P@@](=O)(…`
NSP	1T9B	P07342	138.2 Da LogP -0.17 TPSA 77.8	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN`
OXY	5IMS	P07342	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`
P22	1T9B	P07342	206.0 Da LogP 0.23 TPSA 113.3	✓ Ro5	✓ Clean	`CCO[P@](=O)(O)OP(=O)(O)O`
P23	1T9A	P07342	220.1 Da LogP 0.62 TPSA 113.3	✓ Ro5	✓ Clean	`CCCO[P@@](=O)(O)OP(=O)(O)O`
P25	1T9B	P07342	248.1 Da LogP 1.40 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCO[P@@](=O)(O)OP(=O)(O)O`
PXD	5WKC	P07342	483.4 Da LogP 2.61 TPSA 116.9	✓ Ro5	✓ Clean	`COc1cnc(n2c1nc(n2)NS(=O)(=O)c3c(cccc3OCC(F)F)C(…`
PYD	1T9D	P07342	123.2 Da LogP 0.68 TPSA 51.8	✓ Ro5	✓ Clean	`Cc1cnc(nc1N)C`
PYR	6BD9	P07342	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
RMN	1MCZ	P20906	152.1 Da LogP 0.80 TPSA 57.5	✓ Ro5	✓ Clean	`c1ccc(cc1)[C@H](C(=O)O)O`
TP9	5WKC	P07342	412.3 Da LogP -0.03 TPSA 182.8	1 viol.	✓ Clean	`Cc1ncc(c(n1)N)CN/C(=C(/CCO[P@](=O)([O-])O[P@@](…`
TZD	1PI3	P20906	440.3 Da LogP 0.72 TPSA 187.1	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN2C(=C(SC2=O)CCO[P@@](=O)(O)OP(=…`
YF3	1T9A	P07342	212.3 Da LogP 0.78 TPSA 63.8	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CNC(C)CS`
YF4	1T9A	P07342	180.3 Da LogP 0.82 TPSA 55.0	✓ Ro5	✓ Clean	`CCN(C)Cc1cnc(nc1N)C`

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
CHEMBL2313155	P07342	7.50	414.4 Da LogP -0.09 TPSA 163.6	1 viol.	✓ Clean	`CCOC(=O)c1cnn(C)c1S(=O)(=O)NC(=O)Nc1nc(OC)cc(OC…`
CHEMBL2313153	P07342	7.19	398.4 Da LogP 1.34 TPSA 138.0	✓ Ro5	✓ Clean	`CCOc1ccccc1OS(=O)(=O)NC(=O)Nc1nc(OC)cc(OC)n1`
1CS	P07342	6.90	357.8 Da LogP 1.35 TPSA 123.2	✓ Ro5	✓ Clean	`Cc1nc(nc(n1)OC)NC(=O)NS(=O)(=O)c2ccccc2Cl`
CHEMBL1885280	P07342	6.46	410.4 Da LogP 0.61 TPSA 161.5	✓ Ro5	✓ Clean	`CCOc1nc(NC)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)n1`
1TB	P07342	6.40	395.4 Da LogP 0.51 TPSA 140.7	✓ Ro5	✓ Clean	`Cc1nc(nc(n1)OC)N(C)C(=O)NS(=O)(=O)c2ccccc2C(=O)…`

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
ZINC12501520	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC13540298	1.000	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…`
ZINC13827750	1.000	483.4 Da LogP 2.61 TPSA 116.9	✓ Ro5	✓ Clean	`COc1cnc(OC)n2nc(NS(=O)(=O)c3c(OCC(F)F)cccc3C(F)…`
ZINC1580161	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC2382739	1.000	418.3 Da LogP 2.56 TPSA 107.7	✓ Ro5	✓ Clean	`COc1cc(OC)n2nc(S(=O)(=O)Nc3c(Cl)ccc(C)c3Cl)nc2n1`
ZINC34317654	1.000	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3874716	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC44076059	1.000	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4521548	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC900590	1.000	414.8 Da LogP 1.83 TPSA 136.6	✓ Ro5	✓ Clean	`CCOC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc1nc(Cl)cc(OC)n1`
ZINC103194086	0.845	433.4 Da LogP 1.97 TPSA 116.9	✓ Ro5	✓ Clean	`COc1cccc(C(F)(F)F)c1S(=O)(=O)Nc1nc2c(OC)cnc(OC)…`
ZINC5463312	0.800	234.1 Da LogP 1.28 TPSA 102.3	✓ Ro5	✓ Clean	`CCO[P@](=O)(O)O[P@](=O)(O)OCC`
ZINC1854808	0.795	350.4 Da LogP 1.30 TPSA 138.3	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)O)n1`
ZINC3639593	0.795	365.4 Da LogP 0.79 TPSA 140.2	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc1nc(C)nc(C)n1`
ZINC34140163	0.789	226.2 Da LogP -0.08 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H](O)c1ccc([C@H](O)C(=O)O)cc1`
ZINC34140164	0.789	226.2 Da LogP -0.08 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H](O)c1ccc([C@@H](O)C(=O)O)cc1`
ZINC34140165	0.789	226.2 Da LogP -0.08 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)[C@H](O)c1ccc([C@@H](O)C(=O)O)cc1`
ZINC38334558	0.770	421.3 Da LogP 2.10 TPSA 107.7	✓ Ro5	✓ Clean	`COc1cnc(OC)n2nc(NS(=O)(=O)c3c(F)cccc3C(F)(F)F)n…`
ZINC2522710	0.760	238.3 Da LogP 3.50 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCOP(=O)(O)OCCCCC`
ZINC98050685	0.759	414.4 Da LogP -0.93 TPSA 158.8	1 viol.	✓ Clean	`COC(=O)c1ccccc1S(=O)(=O)NC(=O)n1nc(OC[C@H](C)O)…`
ZINC98050686	0.759	414.4 Da LogP -0.93 TPSA 158.8	1 viol.	✓ Clean	`COC(=O)c1ccccc1S(=O)(=O)NC(=O)n1nc(OC[C@@H](C)O…`
ZINC1561867	0.739	228.2 Da LogP 2.47 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)[C@@H](O)c1ccc(-c2ccccc2)cc1`
ZINC2046525	0.739	228.2 Da LogP 2.47 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)[C@H](O)c1ccc(-c2ccccc2)cc1`
ZINC3176576	0.727	320.4 Da LogP 1.91 TPSA 101.0	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C)n1`
ZINC575419714	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
ZINC115163232	0.700	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC258837490	0.700	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC300799	0.696	340.8 Da LogP 2.26 TPSA 101.0	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)n1`
ZINC115086873	0.688	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC137432264	0.688	457.6 Da LogP -0.91 TPSA 129.3	1 viol.	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC146143823	0.688	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC1692489	0.688	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC1857792028	0.688	430.6 Da LogP 0.04 TPSA 94.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC1857792057	0.688	474.6 Da LogP 0.06 TPSA 103.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC230494776	0.688	325.4 Da LogP -0.96 TPSA 101.6	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCO`
ZINC4530388	0.688	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5701172	0.688	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861	0.688	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC6403917	0.688	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC77271182	0.688	281.3 Da LogP -0.98 TPSA 92.4	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCO`
ZINC83253921	0.688	369.5 Da LogP -0.95 TPSA 110.9	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC90741446	0.688	386.5 Da LogP 0.02 TPSA 84.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90741447	0.688	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`

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.