Protein profile

PA1583

succinate dehydrogenase flavoprotein subunit

Genome: NC_002516.2

Gene: sdhA PA1583 Structure source: AlphaFold UniProt Q9I3D5

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Amino acids 590

Annotations 11

Features 29

PDB binders 34

Druggability 0.387

Overview

Basic information about this protein and its source genome.

Accession: PA1583
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: sdhA PA1583
Status: annotated
Amino acids: 590
Structure source: AlphaFold

1.3.5.1

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: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: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:0008177 Catalysis of the reaction: a quinone + succinate = a quinol + fumarate. GO:0000104 Catalysis of the reaction: succinate + acceptor = fumarate + reduced acceptor. GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 62.816
Human E-value: 2.28e-119
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: CytoplasmicMembrane

Selected Druggability evidence

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 0.387

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1.3.5.1

Gene Ontology (GO)

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: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: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:0008177 Catalysis of the reaction: a quinone + succinate = a quinol + fumarate.
GO:0000104 Catalysis of the reaction: succinate + acceptor = fumarate + reduced acceptor.
GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.
GO:0022900 A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors.
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: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: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.

29 records

Show feature table

Start	End	DB	Term	Name
44	53	ProSitePatterns	PS00504	Fumarate reductase / succinate dehydrogenase FAD-binding site.
44	53	InterPro	IPR003952	Fumarate reductase/succinate dehydrogenase, FAD-binding site
433	549	Gene3D	G3DSA:1.20.58.100	-
482	502	Coils	Coil	Coil
249	352	Gene3D	G3DSA:3.90.700.10	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
249	352	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
249	352	FunFam	G3DSA:3.90.700.10:FF:000001	Mitochondrial succinate dehydrogenase flavoprotein subunit
240	358	SUPERFAMILY	SSF56425	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
240	358	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
550	590	Gene3D	G3DSA:4.10.80.40	succinate dehydrogenase protein domain
454	590	SUPERFAMILY	SSF46977	Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain
454	590	InterPro	IPR037099	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamily
8	590	NCBIfam	TIGR01816	succinate dehydrogenase flavoprotein subunit
8	590	InterPro	IPR011281	Succinate dehydrogenase, flavoprotein subunit
463	590	Pfam	PF02910	Fumarate reductase flavoprotein C-term
463	590	InterPro	IPR015939	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal
6	427	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
6	427	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
550	590	FunFam	G3DSA:4.10.80.40:FF:000001	Succinate dehydrogenase flavoprotein subunit
1	580	PIRSF	PIRSF000171	SDHA_APRA_LASPO
433	549	FunFam	G3DSA:1.20.58.100:FF:000001	Succinate dehydrogenase flavoprotein subunit (SdhA)
10	407	Pfam	PF00890	FAD binding domain
10	407	InterPro	IPR003953	FAD-dependent oxidoreductase 2, FAD binding domain
10	590	NCBIfam	TIGR01812	succinate dehydrogenase or fumarate reductase, flavoprotein subunit
10	590	InterPro	IPR014006	Succinate dehydrogenase/fumarate reductase, flavoprotein subunit
10	418	Gene3D	G3DSA:3.50.50.60	-
10	418	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
8	589	PANTHER	PTHR11632	SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT
8	589	InterPro	IPR030664	FAD-dependent oxidoreductase SdhA/FrdA/AprA

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 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA1583	AlphaFold	—	—	full sequence	—	Viewing

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				0.209

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.

84 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
12J	4YSZ	Q33862	381.2 Da LogP 4.33 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(c1)NC(=O)c2ccccc2I`
3NP	1ZP0	Q0QF01	119.1 Da LogP -0.26 TPSA 80.4	✓ Ro5	✓ Clean	`C(C[N+](=O)[O-])C(=O)O`
3PE	6MYO	Q9YHT1	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
4YP	5C2T	Q33862	303.4 Da LogP 3.35 TPSA 69.4	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)N)OC)C/C=C(\C)/CCC=C(C)C`
AT5	2ACZ	P0AC41	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)[…`
BOL	3AED	Q0QF01	323.1 Da LogP 3.54 TPSA 29.1	✓ Ro5	✓ Clean	`c1ccc(cc1)NC(=O)c2ccccc2I`
CBE	2WDQ	P0AC41	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(SCCO1)C(=O)Nc2ccccc2`
CDN	1NEK	P0AC41	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	P0AC41	282.3 Da LogP 3.89 TPSA 106.5	✓ Ro5	✓ Clean	`CCCCCC(C)c1cc(cc(c1O)[N+](=O)[O-])[N+](=O)[O-]`
E23	4YSX	Q33862	335.4 Da LogP 4.93 TPSA 29.1	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(cc1)CNC(=O)c2ccccc2C(F)(F)F`
E24	4YSY	Q33862	348.2 Da LogP 4.94 TPSA 29.1	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)NCc2ccc(cc2Cl)Cl)C(F)(F)F`
EPH	3VRA	Q33862	709.9 Da LogP 10.16 TPSA 134.4	2 viol.	✓ Clean	`CCCC=CCC=CCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC=CCC…`
F3S	3VRA	Q33862	295.8 Da LogP 2.59 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]2S[Fe]3[S]2[Fe]1S3`
F6A	4YTM	Q33862	341.3 Da LogP 5.62 TPSA 29.1	1 viol.	✓ Clean	`c1ccc(cc1)c2cccc(c2)NC(=O)c3ccccc3C(F)(F)F`
F7A	3AEB	Q0QF01	357.3 Da LogP 5.75 TPSA 38.3	1 viol.	✓ Clean	`c1ccc(cc1)Oc2cccc(c2)NC(=O)c3ccccc3C(F)(F)F`
F9A	3AEA	Q0QF01	322.3 Da LogP 4.02 TPSA 32.3	✓ Ro5	✓ Clean	`CN(C)Cc1cccc(c1)NC(=O)c2ccccc2C(F)(F)F`
FD8	4YTN	Q33862	447.3 Da LogP 6.45 TPSA 38.3	1 viol.	✓ Clean	`c1ccc(c(c1)C(=O)Nc2cccc(c2)Oc3c(c(c(c(c3F)F)F)F…`
FES	3VRA	Q33862	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
FTN	6MYO	Q9YHT1	323.3 Da LogP 4.74 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(c1)NC(=O)c2ccccc2C(F)(F)F`
FUM	3VRB	Q33862	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
MLI	3VRA	Q33862	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MRN	4YT0	Q33862	269.3 Da LogP 4.03 TPSA 38.3	✓ Ro5	✓ Clean	`Cc1ccccc1C(=O)Nc2cccc(c2)OC(C)C`
N1M	3AE4	Q0QF01	261.1 Da LogP 1.65 TPSA 29.1	✓ Ro5	✓ Clean	`CNC(=O)c1ccccc1I`
OAA	6MYO	Q9YHT1	131.1 Da LogP -2.22 TPSA 94.5	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)C(=O)[O-]`
PCI	2WDR	P0AC41	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`c1(c(c(c(c(c1Cl)Cl)Cl)Cl)Cl)O`
RQX	3VR8	Q33862	263.3 Da LogP 2.41 TPSA 69.4	✓ Ro5	Alert	`CCC/C(=C/CC1=C(C(=O)C(=C(C1=O)OC)N)C)/C`
SLI	3AE2	Q0QF01	213.2 Da LogP 2.64 TPSA 49.3	✓ Ro5	✓ Clean	`c1ccc(cc1)NC(=O)c2ccccc2O`
TEO	2WDQ	P0AC41	132.1 Da LogP -3.14 TPSA 103.7	✓ Ro5	✓ Clean	`C(=C(\O)/[O-])\[C@H](C(=O)[O-])O`
TFZ	3AE1	Q0QF01	265.2 Da LogP 3.96 TPSA 29.1	✓ Ro5	✓ Clean	`c1ccc(cc1)NC(=O)c2ccccc2C(F)(F)F`
TMG	3SFE	Q0QF01	201.3 Da LogP 2.69 TPSA 41.6	✓ Ro5	✓ Clean	`c1ccc2c(c1)[nH]c(n2)c3cscn3`
TTF	1ZP0	Q0QF01	222.2 Da LogP 2.45 TPSA 34.1	✓ Ro5	✓ Clean	`c1cc(sc1)C(=O)CC(=O)C(F)(F)F`
UMQ	6MYO	Q9YHT1	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)…`
UQ1	5C3J	Q33862	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C`
UQ2	1NEK	P0AC41	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
ZINC100004957	1.000	222.2 Da LogP 2.45 TPSA 34.1	✓ Ro5	✓ Clean	`O=C(CC(=O)C(F)(F)F)c1cccs1`
ZINC100053689	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC100053691	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC102190506	1.000	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	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC1479	1.000	323.3 Da LogP 4.74 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(NC(=O)c2ccccc2C(F)(F)F)c1`
ZINC1501015302	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
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`
ZINC2039285652	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285653	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285654	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285655	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2053493146	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493147	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493148	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493149	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC238809244	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC238809245	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC252695223	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695224	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695225	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695226	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC43478	1.000	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2)SCCO1`
ZINC58649715	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC59978443	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](…`
ZINC66157001	1.000	468.5 Da LogP -1.62 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC70669940	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669941	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669942	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669943	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC73711	1.000	201.3 Da LogP 2.69 TPSA 41.6	✓ Ro5	✓ Clean	`c1ccc2[nH]c(-c3cscn3)nc2c1`
ZINC77311968	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H]…`
ZINC83433913	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](CO…`
ZINC85482724	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC86002923	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@H](O[C@H]2O[C@H](CO)…`
ZINC27416437	0.976	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	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
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`
ZINC100623039	0.811	334.5 Da LogP 1.33 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)…`
ZINC100623040	0.811	334.5 Da LogP 1.33 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](O…`
ZINC118906375	0.811	264.3 Da LogP -0.62 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H]1O`
ZINC141152247	0.811	264.3 Da LogP -0.62 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H]…`
ZINC48016017	0.811	278.3 Da LogP -0.23 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]…`
ZINC5820343	0.811	264.3 Da LogP -0.62 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O`

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.