Protein profile

KP13_31481

Fumarate reductase flavoprotein subunit

Genome: KpKP13

Gene: frdA AHE46751.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GI02

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Amino acids 596

Annotations 10

Features 42

PDB binders 36

Druggability 0.997

Overview

Basic information about this protein and its source genome.

Accession: KP13_31481
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: frdA AHE46751.1
Status: annotated
Amino acids: 596
Structure source: AlphaFold + ColabFold

1.3.5.1

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: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. 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: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: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:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 43.99
Human E-value: 2.57e-100
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 54.352
DEG E-value: 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 96.29

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 0.997

Structure A0A0H3GI02

Pocket Pocket 1

P2Rank 0.975

Structure A0A0H3GI02

Pocket Pocket 1

ColabFold model

FPocket 0.737 · Pocket 1

P2Rank 0.983 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 157 / 4744 genomes with a hit

Normalized 0.033

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1.3.5.1

Gene Ontology (GO)

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: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.
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: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: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: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:0008177 Catalysis of the reaction: a quinone + succinate = a quinol + fumarate.
GO:0006113 The metabolic process that uses oxidation-reduction reactions of organic compounds and substrate-level phosphorylation for the generation of adenosine triphosphate (ATP), without consuming oxygen and is independent of electron transport chains.

Sequence Features

Domain/signature hits from InterPro and related databases.

42 records

Show feature table

Start	End	DB	Term	Name
28	596	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
237	366	Gene3D	G3DSA:3.90.700.10	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
237	366	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
8	18	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
543	577	Gene3D	G3DSA:4.10.80.40	succinate dehydrogenase protein domain
19	27	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	7	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
434	490	CDD	cd00167	SANT
434	490	InterPro	IPR001005	SANT/Myb domain
423	443	Coils	Coil	Coil
7	251	FunFam	G3DSA:3.50.50.60:FF:000017	Fumarate reductase flavoprotein subunit
543	577	FunFam	G3DSA:4.10.80.40:FF:000003	Fumarate reductase flavoprotein subunit
375	382	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
7	29	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
7	581	NCBIfam	TIGR01812	succinate dehydrogenase or fumarate reductase, flavoprotein subunit
7	581	InterPro	IPR014006	Succinate dehydrogenase/fumarate reductase, flavoprotein subunit
227	358	SUPERFAMILY	SSF56425	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
227	358	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
7	397	Pfam	PF00890	FAD binding domain
7	397	InterPro	IPR003953	FAD-dependent oxidoreductase 2, FAD binding domain
2	416	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
2	416	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	574	PIRSF	PIRSF000171	SDHA_APRA_LASPO
453	581	Pfam	PF02910	Fumarate reductase flavoprotein C-term
453	581	InterPro	IPR015939	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal
43	52	ProSitePatterns	PS00504	Fumarate reductase / succinate dehydrogenase FAD-binding site.
43	52	InterPro	IPR003952	Fumarate reductase/succinate dehydrogenase, FAD-binding site
360	382	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
8	27	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
423	542	Gene3D	G3DSA:1.20.58.100	-
424	540	FunFam	G3DSA:1.20.58.100:FF:000001	Succinate dehydrogenase flavoprotein subunit (SdhA)
237	366	FunFam	G3DSA:3.90.700.10:FF:000003	Fumarate reductase flavoprotein subunit
473	493	Coils	Coil	Coil
5	575	PANTHER	PTHR11632	SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT
5	575	InterPro	IPR030664	FAD-dependent oxidoreductase SdhA/FrdA/AprA
444	590	SUPERFAMILY	SSF46977	Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain
444	590	InterPro	IPR037099	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamily
7	409	Gene3D	G3DSA:3.50.50.60	-
7	409	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	27	Phobius	SIGNAL_PEPTIDE	Signal peptide region
3	582	NCBIfam	TIGR01176	fumarate reductase (quinol) flavoprotein subunit
3	582	InterPro	IPR005884	Fumarate reductase, flavoprotein subunit

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_A0A0H3GI02	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_31481	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				0.997
22				0.862
19				0.69

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	30.87	0.936
2	8.55	0.457
3	7.12	0.369
4	6.22	0.311
5	1.98	0.042

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				0.737
13				0.218

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	32.42	0.943
2	8.94	0.479
3	8.22	0.438
4	8.18	0.435
5	2.18	0.052

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.

86 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
3NP	3P4S	P00363	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…`
AT5	6MYS	Q9YHT1	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`
BRS	1KFY	P00363	322.7 Da LogP 4.01 TPSA 106.5	✓ Ro5	✓ Clean	`C[C@H](c1ccc(cc1)Cl)c2cc(cc(c2O)[N+](=O)[O-])[N…`
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…`
CE1	1KF6	P00363	538.8 Da LogP 4.03 TPSA 94.1	1 viol.	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCOCCO`
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-]`
EPH	1NEK	P0AC41	709.9 Da LogP 10.16 TPSA 134.4	2 viol.	✓ Clean	`CCCC=CCC=CCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC=CCC…`
F3S	1KF6	P00363	295.8 Da LogP 2.59 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]2S[Fe]3[S]2[Fe]1S3`
F6A	3ABV	Q0QF01	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	3AE9	Q0QF01	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	1KF6	P00363	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
FLC	2B76	P00363	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
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	3P4P	P00363	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
GUA	3P4R	P00363	132.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)CC(=O)O`
HQO	1KF6	P00363	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(c2ccccc2[n+]1[O-])O`
LMT	5XMJ	T2GB49	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1…`
MLI	6B58	P00363	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MQ7	1L0V	P00363	649.0 Da LogP 14.10 TPSA 34.1	2 viol.	Alert	`CC1=C(C(=O)c2ccccc2C1=O)C\C=C(/C)\CC\C=C(/C)\CC…`
MRN	3AE5	Q0QF01	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	1KF6	P00363	131.1 Da LogP -2.22 TPSA 94.5	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)C(=O)[O-]`
PBF	6B58	P00363	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)c2ccc(cc2)C[C@@H](C(=O)O)N`
PCI	3SFD	Q0QF01	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`c1(c(c(c(c(c1Cl)Cl)Cl)Cl)Cl)O`
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)…`
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
ZINC100014200	1.000	494.7 Da LogP 4.02 TPSA 84.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCO`
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…`
ZINC100070166	1.000	290.4 Da LogP 3.17 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCO`
ZINC100310628	1.000	478.7 Da LogP 4.78 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC100365196	1.000	302.5 Da LogP 4.71 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCO`
ZINC101772322	1.000	434.7 Da LogP 4.76 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC103600921	1.000	466.7 Da LogP 3.24 TPSA 84.8	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1479	1.000	323.3 Da LogP 4.74 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(NC(=O)c2ccccc2C(F)(F)F)c1`
ZINC14880431	1.000	378.6 Da LogP 3.20 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC14881140	1.000	306.4 Da LogP 2.41 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCO`
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`
ZINC1529909	1.000	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(O)c2ccccc2[n+]1[O-]`
ZINC16051619	1.000	350.5 Da LogP 2.42 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCOCCO`
ZINC173184	1.000	261.1 Da LogP 1.65 TPSA 29.1	✓ Ro5	✓ Clean	`CNC(=O)c1ccccc1I`
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…`
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…`
ZINC2561081	1.000	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC2561082	1.000	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC2584424	1.000	218.3 Da LogP 2.37 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCO`
ZINC43478	1.000	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2)SCCO1`
ZINC4521877	1.000	234.3 Da LogP 1.61 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCOCCOCCOCCO`
ZINC5273610	1.000	322.4 Da LogP 1.64 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCOCCOCCOCCOCCOCCO`
ZINC58538366	1.000	392.6 Da LogP 3.59 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC58631420	1.000	422.6 Da LogP 3.22 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
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@…`
ZINC59441819	1.000	318.5 Da LogP 3.95 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCO`
ZINC59622400	1.000	274.4 Da LogP 3.93 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCO`
ZINC61524	1.000	323.1 Da LogP 3.54 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)c1ccccc1I`
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@…`
ZINC71788551	1.000	334.5 Da LogP 3.19 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCO`
ZINC71788564	1.000	262.4 Da LogP 2.39 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCO`
ZINC71788567	1.000	406.6 Da LogP 3.98 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC73711	1.000	201.3 Da LogP 2.69 TPSA 41.6	✓ Ro5	✓ Clean	`c1ccc2[nH]c(-c3cscn3)nc2c1`
ZINC8214594	1.000	362.6 Da LogP 3.97 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCO`
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…`
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)…`
ZINC88260008	1.000	390.6 Da LogP 4.75 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCO`
ZINC95784968	1.000	450.7 Da LogP 4.00 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC95863931	1.000	464.7 Da LogP 4.39 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`

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.