Protein profile

KP13_31513

Indole-3-pyruvate decarboxylase

Genome: KpKP13

Gene: AHE43376.1 ipdC Structure source: AlphaFold + ColabFold UniProt A0A0H3GRC2

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Amino acids 555

Annotations 7

Features 25

PDB binders 15

Druggability 0.615

Overview

Basic information about this protein and its source genome.

Accession: KP13_31513
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43376.1 ipdC
Status: annotated
Amino acids: 555
Structure source: AlphaFold + ColabFold

GO:0016831 Catalysis of the nonhydrolytic addition or removal of a carboxyl group to or from a compound. 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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0004737 Catalysis of the reaction: a 2-oxo acid = an aldehyde + CO2.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 43.433
DEG E-value: 1.82e-171
Localization: CytoplasmicMembrane
ColabFold pLDDT: 95.7

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 0.615

Structure A0A0H3GRC2

Pocket Pocket 5

P2Rank 0.403

Structure A0A0H3GRC2

Pocket Pocket 1

ColabFold model

FPocket 0.861 · Pocket 1

P2Rank 0.495 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 66 / 4744 genomes with a hit

Normalized 0.014

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

GO:0016831 Catalysis of the nonhydrolytic addition or removal of a carboxyl group to or from a compound.
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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0004737 Catalysis of the reaction: a 2-oxo acid = an aldehyde + CO2.
GO:0000949 The chemical reactions and pathways involving the catabolism of aromatic amino acids to produce aromatic alcohols with one carbon less than the starting amino acid. In S. cerevisiae, this is known to occur for leucine, isoleucine, valine, methionine, phenylalanine, tyrosine, or tryptophan. When an aromatic family amino acid, phenylalanine, tyrosine, or tryptophan, is used as the substrate, 2-phenylethanol, 4-hydroxyphenylethanol, or tryptophol, respectively, is produced. Often referred to as the Ehrlich pathway, these reactions generally occur during fermentation to produce a variety of alcohols, often collectively referred to as fusel alcohols. Depending on the redox state of the cells, carboxylic acid derivatives may be produced instead of alcohols.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
353	545	FunFam	G3DSA:3.40.50.970:FF:000024	Pyruvate decarboxylase isozyme
8	177	Pfam	PF02776	Thiamine pyrophosphate enzyme, N-terminal TPP binding domain
8	177	InterPro	IPR012001	Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
5	188	FunFam	G3DSA:3.40.50.970:FF:000019	Pyruvate decarboxylase isozyme
359	546	Gene3D	G3DSA:3.40.50.970	-
7	178	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
7	178	InterPro	IPR029061	Thiamin diphosphate-binding fold
11	170	CDD	cd07038	TPP_PYR_PDC_IPDC_like
11	170	InterPro	IPR047213	Pyruvate decarboxylase/indolepyruvate decarboxylase-like, pyrimidine-binding domain
362	542	CDD	cd02005	TPP_PDC_IPDC
362	542	InterPro	IPR047214	Pyruvate decarboxylase/indolepyruvate decarboxylase-like, PP-binding domain
190	349	Gene3D	G3DSA:3.40.50.1220	-
360	546	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
360	546	InterPro	IPR029061	Thiamin diphosphate-binding fold
202	319	Pfam	PF00205	Thiamine pyrophosphate enzyme, central domain
202	319	InterPro	IPR012000	Thiamine pyrophosphate enzyme, central domain
396	530	Pfam	PF02775	Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
396	530	InterPro	IPR011766	Thiamine pyrophosphate enzyme, TPP-binding
4	544	PANTHER	PTHR43452	PYRUVATE DECARBOXYLASE
4	544	InterPro	IPR012110	Pyruvate decarboxylase/indolepyruvate decarboxylase-like
169	339	SUPERFAMILY	SSF52467	DHS-like NAD/FAD-binding domain
169	339	InterPro	IPR029035	DHS-like NAD/FAD-binding domain superfamily
4	186	Gene3D	G3DSA:3.40.50.970	-
2	554	PIRSF	PIRSF036565	Pyruvt_ip_decrb
2	554	InterPro	IPR012110	Pyruvate decarboxylase/indolepyruvate decarboxylase-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_A0A0H3GRC2	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_31513	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
6				0.131
16				0.006
1				0.002
2				0.001

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	8.8	0.403
2	5.23	0.2
3	4.66	0.167
4	2.18	0.043
5	1.47	0.017

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
1				0.861

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	6.21	0.31
2	2.73	0.082
3	2.48	0.068
4	2.16	0.051
5	2.12	0.049

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.

68 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
2OP	2VK8	P06169	90.1 Da LogP -0.55 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)O`
ALK	2VJY	Q12629	140.1 Da LogP 0.16 TPSA 66.8	✓ Ro5	✓ Clean	`C[C@H](O)P(=O)(O)OC`
ALU	2VJY	Q12629	138.1 Da LogP 0.36 TPSA 63.6	✓ Ro5	✓ Clean	`CC(=O)[P@](=O)(O)OC`
DPX	1ZPD	P06672	430.3 Da LogP 0.21 TPSA 197.3	1 viol.	✓ Clean	`Cc1ncc(c(n1)N)CN/C(=C(/[C@@H](CO[P@](=O)(O)OP(=…`
KPV	2Q5Q	P51852	192.2 Da LogP 1.66 TPSA 54.4	✓ Ro5	✓ Clean	`c1ccc(cc1)CCCC(=O)C(=O)O`
PPY	2Q5O	P51852	164.2 Da LogP 0.88 TPSA 54.4	✓ Ro5	✓ Clean	`c1ccc(cc1)CC(=O)C(=O)O`
PY0	2W93	P06169	106.1 Da LogP -2.67 TPSA 89.5	✓ Ro5	✓ Clean	`C[C@@H]([C@@](N)(O)[O-])O`
PYM	1QPB	P06169	87.1 Da LogP -0.94 TPSA 60.2	✓ Ro5	✓ Clean	`CC(=O)C(=O)N`
PYR	2VK1	P06169	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
R1T	2Q5L	P51852	467.4 Da LogP 2.15 TPSA 185.3	✓ Ro5	✓ Clean	`Cc1c(sc(c1Cc2cnc(nc2N)C)[C@@H](C)O)CCO[P@](=O)(…`
S1T	2Q5L	P51852	467.4 Da LogP 2.15 TPSA 185.3	✓ Ro5	✓ Clean	`Cc1c(sc(c1Cc2cnc(nc2N)C)[C@H](C)O)CCO[P@](=O)(O…`
TDL	3OE1	P06672	513.4 Da LogP 0.13 TPSA 226.5	2 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@](C)(C(=O)O)O)CCO…`
TLA	2Q5Q	P51852	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=O)O)O`
TPU	2WVA	P06672	408.2 Da LogP 0.08 TPSA 195.8	✓ Ro5	✓ Clean	`Cc1c(nnn1Cc2cnc(nc2N)C)CCO[P@](=O)(O)OP(=O)(O)O`
TPW	2Q5J	P51852	423.3 Da LogP 2.10 TPSA 165.1	✓ Ro5	✓ Clean	`Cc1c(csc1CCO[P@@](=O)(O)OP(=O)(O)O)Cc2cnc(nc2N)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
CHEMBL3559521	P06672	10.52	394.2 Da LogP -0.22 TPSA 195.8	✓ Ro5	✓ Clean	`Cc1ncc(Cn2cc(CCOP(=O)(O)OP(=O)(O)O)nn2)c(N)n1`
1CS	J7HAW4	8.15	357.8 Da LogP 1.35 TPSA 123.2	✓ Ro5	✓ Clean	`Cc1nc(nc(n1)OC)NC(=O)NS(=O)(=O)c2ccccc2Cl`
CHEMBL401913	J7HAW4	7.64	350.4 Da LogP 1.30 TPSA 138.3	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)O)n1`

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
ZINC1854808	1.000	350.4 Da LogP 1.30 TPSA 138.3	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)O)n1`
ZINC1602735	0.800	238.3 Da LogP 2.61 TPSA 34.1	✓ Ro5	Alert	`O=C(Cc1ccccc1)C(=O)Cc1ccccc1`
ZINC186159	0.792	337.4 Da LogP 1.01 TPSA 123.2	✓ Ro5	✓ Clean	`COc1nc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C)n1`
ZINC22016278	0.765	461.1 Da LogP 2.87 TPSA 123.2	✓ Ro5	✓ Clean	`COc1nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)nc(C(Cl)(Cl)C…`
ZINC2521491	0.765	373.8 Da LogP 1.06 TPSA 143.4	✓ Ro5	✓ Clean	`COc1nc(C)nc(NC(=O)NS(=O)(=O)c2cc(O)ccc2Cl)n1`
ZINC103209083	0.761	336.3 Da LogP 0.99 TPSA 138.3	✓ Ro5	✓ Clean	`Cc1ccnc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)O)n1`
ZINC22219569	0.750	240.3 Da LogP 2.55 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)C(=O)Cc1ccc(-c2ccccc2)cc1`
ZINC3176576	0.744	320.4 Da LogP 1.91 TPSA 101.0	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C)n1`
ZINC300799	0.711	340.8 Da LogP 2.26 TPSA 101.0	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)n1`
ZINC1532902	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC12359024	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC18193628	0.692	370.8 Da LogP 1.41 TPSA 117.2	✓ Ro5	✓ Clean	`Cc1nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)nc(N(C)C)n1`
ZINC2013424	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC22204870	0.684	409.8 Da LogP 2.30 TPSA 136.3	✓ Ro5	✓ Clean	`COc1nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)nc(-c2ccco2)n1`
ZINC3149462	0.660	371.8 Da LogP 1.38 TPSA 114.4	✓ Ro5	✓ Clean	`COc1nc(C)nc(N(C)C(=O)NS(=O)(=O)c2ccccc2Cl)n1`
ZINC902231	0.660	357.8 Da LogP 1.56 TPSA 126.7	✓ Ro5	✓ Clean	`COc1nc(C)nc(N/C(O)=N\S(=O)(=O)c2ccccc2Cl)n1`
ZINC6580259	0.655	270.3 Da LogP 2.46 TPSA 63.6	✓ Ro5	✓ Clean	`O=C(O)C(=O)Cc1ccc(OCc2ccccc2)cc1`
ZINC1226893	0.655	440.7 Da LogP 2.53 TPSA 123.2	✓ Ro5	✓ Clean	`COc1nc(NC(=O)NS(=O)(=O)c2ccccc2C)nc(C(Cl)(Cl)Cl…`
ZINC3593496	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC13540298	0.645	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…`
ZINC58002826	0.645	206.2 Da LogP 1.75 TPSA 43.4	✓ Ro5	✓ Clean	`COC(=O)C(=O)CCCc1ccccc1`
ZINC19256938	0.640	243.1 Da LogP 1.65 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)C(=O)Cc1ccc(Br)cc1`
ZINC1679978	0.636	210.3 Da LogP 3.04 TPSA 17.1	✓ Ro5	✓ Clean	`O=C(Cc1ccccc1)Cc1ccccc1`
ZINC3848736	0.633	340.8 Da LogP 2.26 TPSA 101.0	✓ Ro5	✓ Clean	`Cc1cc(Cl)nc(NC(=O)NS(=O)(=O)c2ccccc2C)n1`
ZINC3639593	0.627	365.4 Da LogP 0.79 TPSA 140.2	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc1nc(C)nc(C)n1`
ZINC14686440	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC1712441	0.621	224.3 Da LogP 3.89 TPSA 17.1	✓ Ro5	✓ Clean	`O=C(CCCc1ccccc1)c1ccccc1`
ZINC1693912	0.615	266.3 Da LogP 3.39 TPSA 34.1	✓ Ro5	Alert	`O=C(CCc1ccccc1)C(=O)CCc1ccccc1`
ZINC22016266	0.614	484.7 Da LogP 2.00 TPSA 149.5	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc1nc(OC)nc(C(Cl)…`
ZINC22016269	0.614	395.4 Da LogP 0.88 TPSA 149.5	✓ Ro5	✓ Clean	`CCOc1nc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)n1`
ZINC2275141	0.610	421.9 Da LogP 2.15 TPSA 131.8	✓ Ro5	✓ Clean	`Cc1cc(C)n(-c2nc(C)nc(NC(=O)NS(=O)(=O)c3ccccc3Cl…`
ZINC8215517	0.609	425.3 Da LogP 0.84 TPSA 169.0	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCO[P@@](=O)(O)OP(=O)(O)O)c2C)…`
ZINC3848734	0.608	336.4 Da LogP 1.61 TPSA 110.3	✓ Ro5	✓ Clean	`COc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C)n1`
ZINC22016313	0.607	351.4 Da LogP 1.26 TPSA 123.2	✓ Ro5	✓ Clean	`CCc1nc(NC(=O)NS(=O)(=O)c2ccccc2C)nc(OC)n1`
ZINC22016655	0.607	408.2 Da LogP 1.37 TPSA 148.1	✓ Ro5	✓ Clean	`COc1nc(C)nc(NC(=O)NS(=O)(=O)Nc2nc(Cl)ccc2Cl)n1`
ZINC22221925	0.607	243.1 Da LogP 1.65 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)C(=O)Cc1cccc(Br)c1`
ZINC5521335	0.607	214.2 Da LogP 2.04 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)C(=O)Cc1ccc2ccccc2c1`
ZINC34632965	0.606	220.3 Da LogP 2.14 TPSA 43.4	✓ Ro5	✓ Clean	`CCOC(=O)C(=O)CCCc1ccccc1`
ZINC35874338	0.603	493.2 Da LogP 1.00 TPSA 160.5	✓ Ro5	✓ Clean	`COc1nc(C)nc(NC(=O)NS(=O)(=O)c2cc(I)ccc2C(=O)O)n1`

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.