Protein profile

KP13_03281

Succinate dehydrogenase cytochrome b556 subunit

Genome: KpKP13

Gene: AHE45660.1 sdhC Structure source: AlphaFold + ColabFold UniProt A0A0V9SNE0

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Amino acids 134

Annotations 9

Features 28

PDB binders 11

Druggability 0.676

Overview

Basic information about this protein and its source genome.

Accession: KP13_03281
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE45660.1 sdhC
Status: annotated
Amino acids: 134
Structure source: AlphaFold + ColabFold

GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. GO:0045281 OBSOLETE. A multimeric complex which consists of flavoprotein (subunit A ; InterPro:IPR003952), iron-sulfur protein (subunit B) and membrane-bound cytochrome b560 (subunit C; InterPro:IPR000701). In some Archaea, the membrane-bound subunits (C or C and D) do not necessarily contain heme. Membrane-bound subunits can bind or react with quinones. GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. GO:0000104 Catalysis of the reaction: succinate + acceptor = fumarate + reduced acceptor.

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 (%): 64.567
DEG E-value: 2.31e-51
Localization: CytoplasmicMembrane
ColabFold pLDDT: 95.01

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 0.676

Structure A0A0V9SNE0

Pocket Pocket 1

P2Rank 0.068

Structure A0A0V9SNE0

Pocket Pocket 1

ColabFold model

FPocket 0.687 · Pocket 1

P2Rank 0.105 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 107 / 4744 genomes with a hit

Normalized 0.023

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Gene Ontology (GO)

GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0045281 OBSOLETE. A multimeric complex which consists of flavoprotein (subunit A ; InterPro:IPR003952), iron-sulfur protein (subunit B) and membrane-bound cytochrome b560 (subunit C; InterPro:IPR000701). In some Archaea, the membrane-bound subunits (C or C and D) do not necessarily contain heme. Membrane-bound subunits can bind or react with quinones.
GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
GO:0000104 Catalysis of the reaction: succinate + acceptor = fumarate + reduced acceptor.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0046872 Binding to a metal ion.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Sequence Features

Domain/signature hits from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
12	131	NCBIfam	TIGR02970	succinate dehydrogenase, cytochrome b556 subunit
12	131	InterPro	IPR014314	Succinate dehydrogenase, cytochrome b556 subunit
14	131	CDD	cd03499	SQR_TypeC_SdhC
14	131	InterPro	IPR014314	Succinate dehydrogenase, cytochrome b556 subunit
14	38	ProSitePatterns	PS01000	Succinate dehydrogenase cytochrome b subunit signature 1.
14	38	InterPro	IPR018495	Succinate dehydrogenase, cytochrome b subunit, conserved site
33	55	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
33	53	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
77	94	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
114	133	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
11	128	Pfam	PF01127	Succinate dehydrogenase/Fumarate reductase transmembrane subunit
11	128	InterPro	IPR000701	Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit
1	134	PIRSF	PIRSF000178	SDH_cyt_b560
1	134	InterPro	IPR014314	Succinate dehydrogenase, cytochrome b556 subunit
6	134	Gene3D	G3DSA:1.20.1300.10	Fumarate reductase/succinate dehydrogenase, transmembrane subunit
6	134	InterPro	IPR034804	Fumarate reductase/succinate dehydrogenase, transmembrane subunit
6	134	FunFam	G3DSA:1.20.1300.10:FF:000005	Succinate dehydrogenase cytochrome b556 subunit
134	134	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
95	114	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
89	102	ProSitePatterns	PS01001	Succinate dehydrogenase cytochrome b subunit signature 2.
89	102	InterPro	IPR018495	Succinate dehydrogenase, cytochrome b subunit, conserved site
6	134	SUPERFAMILY	SSF81343	Fumarate reductase respiratory complex transmembrane subunits
73	94	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
7	129	PANTHER	PTHR10978	SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT
7	129	InterPro	IPR014314	Succinate dehydrogenase, cytochrome b556 subunit
115	133	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	32	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
54	72	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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_A0A0V9SNE0	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03281	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
1				0.676
3				0.395
4				0.299

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	2.08	0.047
2	1.63	0.027
3	1.43	0.019

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				0.687

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	3.09	0.104
2	2.22	0.054
3	2.08	0.047
4	1.92	0.039

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.

61 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
AT5	2ACZ	P69054	366.2 Da LogP 2.79 TPSA 88.6	✓ Ro5	✓ Clean	`C[C@@H](C[C@H](C)C(=O)C1=C(C(=C(NC1=O)OC)OC)O)[…`
CBE	2WDQ	P69054	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(SCCO1)C(=O)Nc2ccccc2`
CDN	1NEK	P69054	1151.5 Da LogP 14.77 TPSA 249.6	4 viol.	✓ Clean	`CCCCCCCCCCCCCCC(O)O[C@H](COC(CCCCC)O)CO[P@@](=O…`
DNT	1NEN	P69054	282.3 Da LogP 3.89 TPSA 106.5	✓ Ro5	✓ Clean	`CCCCCC(C)c1cc(cc(c1O)[N+](=O)[O-])[N+](=O)[O-]`
EPH	1NEK	P69054	709.9 Da LogP 10.16 TPSA 134.4	2 viol.	✓ Clean	`CCCC=CCC=CCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC=CCC…`
F3S	1NEK	P69054	295.8 Da LogP 2.59 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]2S[Fe]3[S]2[Fe]1S3`
FES	1NEK	P69054	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
OAA	1NEK	P69054	131.1 Da LogP -2.22 TPSA 94.5	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)C(=O)[O-]`
PCI	2WDR	P69054	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`c1(c(c(c(c(c1Cl)Cl)Cl)Cl)Cl)O`
TEO	2WDQ	P69054	132.1 Da LogP -3.14 TPSA 103.7	✓ Ro5	✓ Clean	`C(=C(\O)/[O-])\[C@H](C(=O)[O-])O`
UQ2	1NEK	P69054	318.4 Da LogP 4.04 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)C\C=C(/C)\CCC=C(C)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).

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
ZINC1529471	1.000	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1c(Cl)c(Cl)c(Cl)c(Cl)c1Cl`
ZINC1532641	1.000	318.4 Da LogP 4.04 TPSA 52.6	✓ Ro5	Alert	`COC1=C(OC)C(=O)C(C/C=C(\C)CCC=C(C)C)=C(C)C1=O`
ZINC43478	1.000	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2)SCCO1`
ZINC33649281	0.974	296.3 Da LogP 4.28 TPSA 106.5	✓ Ro5	✓ Clean	`CCCCCC[C@@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-…`
ZINC33649283	0.974	296.3 Da LogP 4.28 TPSA 106.5	✓ Ro5	✓ Clean	`CCCCCC[C@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-]…`
ZINC225408	0.900	247.9 Da LogP 3.71 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1c(Cl)c(Cl)c(O)c(Cl)c1Cl`
ZINC1583639	0.821	254.2 Da LogP 3.11 TPSA 106.5	✓ Ro5	✓ Clean	`CCC[C@@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c…`
ZINC2038099	0.821	254.2 Da LogP 3.11 TPSA 106.5	✓ Ro5	✓ Clean	`CCC[C@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC154748	0.818	247.9 Da LogP 3.71 TPSA 40.5	✓ Ro5	Alert	`Oc1c(O)c(Cl)c(Cl)c(Cl)c1Cl`
ZINC1559692	0.750	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`COC1=C(OC)C(=O)C(CC=C(C)C)=C(C)C1=O`
ZINC13828017	0.725	240.2 Da LogP 2.72 TPSA 106.5	✓ Ro5	✓ Clean	`CC[C@@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC13828020	0.725	240.2 Da LogP 2.72 TPSA 106.5	✓ Ro5	✓ Clean	`CC[C@H](C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC102190506	0.696	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512	0.696	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC27416437	0.679	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364	0.679	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC2513914	0.675	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2)OCCS1`
ZINC32918592	0.652	307.4 Da LogP 2.80 TPSA 64.6	✓ Ro5	✓ Clean	`CCOC(=O)c1ccc(NC(=O)C2=C(C)OCCS2)cc1`
ZINC1687159	0.625	226.2 Da LogP 2.33 TPSA 106.5	✓ Ro5	✓ Clean	`CC(C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC9115226	0.625	360.5 Da LogP 3.64 TPSA 58.6	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(C(=O)N3CCCCCC3)cc2)SCCO1`
ZINC1501016364	0.623	465.6 Da LogP 4.63 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O…`
ZINC20919537	0.612	388.5 Da LogP 4.46 TPSA 67.4	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(C(=O)NC3CCCCCCC3)cc2)SCCO1`
ZINC9115252	0.612	374.5 Da LogP 4.07 TPSA 67.4	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(C(=O)NC3CCCCCC3)cc2)SCCO1`
ZINC9115309	0.612	360.5 Da LogP 3.68 TPSA 67.4	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(C(=O)NC3CCCCC3)cc2)SCCO1`
ZINC6895037	0.604	382.5 Da LogP 3.86 TPSA 67.4	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2cccc(C(=O)NCc3ccccc3C)c2)SCCO1`
ZINC12323380	0.595	297.4 Da LogP 3.76 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C1=C(c2ccccc2)SCCO1`
ZINC6895073	0.588	374.5 Da LogP 3.57 TPSA 58.6	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(CC(=O)N3CCCCCC3)cc2)SCCO1`
ZINC28404190	0.565	311.4 Da LogP 4.07 TPSA 38.3	✓ Ro5	✓ Clean	`Cc1ccc(NC(=O)C2=C(c3ccccc3)SCCO2)cc1`
ZINC98180109	0.563	246.9 Da LogP 3.59 TPSA 46.2	✓ Ro5	✓ Clean	`Nc1c(O)c(Cl)c(Cl)c(Cl)c1Cl`
ZINC1492540	0.558	355.8 Da LogP 3.84 TPSA 64.6	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccc(Cl)c(C(=O)OC(C)C)c2)SCCO1`
ZINC13544781	0.556	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783	0.556	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC12322718	0.543	354.4 Da LogP 3.72 TPSA 67.4	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(NC(=O)C2=C(c3ccccc3)SCCO2)cc1`
ZINC13543439	0.540	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543441	0.540	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC6894966	0.537	374.5 Da LogP 3.61 TPSA 67.4	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2C(=O)NCc2cccs2)SCCO1`
ZINC9115097	0.537	369.4 Da LogP 2.95 TPSA 80.3	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2C(=O)NCc2ccccn2)SCCO1`
ZINC129184	0.533	267.3 Da LogP 1.30 TPSA 72.5	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2)S(=O)(=O)CCO1`
ZINC102190945	0.525	411.5 Da LogP 3.29 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCCN`
ZINC32840692	0.525	425.5 Da LogP 3.68 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCCN`
ZINC32840693	0.525	425.5 Da LogP 3.68 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCCN`
ZINC32840704	0.525	453.6 Da LogP 4.46 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCCN`
ZINC32840705	0.525	453.6 Da LogP 4.46 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCCN`
ZINC95635984	0.525	397.4 Da LogP 2.90 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCCN`
ZINC102191119	0.524	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC33822387	0.524	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC33822389	0.524	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)…`
ZINC58649551	0.524	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC5956205	0.524	212.2 Da LogP 1.77 TPSA 106.5	✓ Ro5	✓ Clean	`CCc1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC2046309	0.523	254.2 Da LogP 3.11 TPSA 106.5	✓ Ro5	✓ Clean	`CCC[C@H](C)c1cc([N+](=O)[O-])c(O)c([N+](=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.