Protein profile

KP13_04654

FAD linked oxidase domain-containing protein

Genome: KpKP13

Gene: AHE44086.1 Structure source: AlphaFold + ColabFold UniProt W8UTR3

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Amino acids 1018

Annotations 10

Features 25

PDB binders 19

Druggability 0.857

Overview

Basic information about this protein and its source genome.

Accession: KP13_04654
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE44086.1
Status: annotated
Amino acids: 1018
Structure source: AlphaFold + ColabFold

1.1.99.39

GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. 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: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:0051990 Catalysis of the reaction: (R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor. GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0004458 Catalysis of the reaction: (R)-lactate + 2 [Fe(III)cytochrome c] = 2 [Fe(II)cytochrome c] + 2 H+ + pyruvate.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 28.889
Human E-value: 7.56e-08
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 87.414
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 93.45

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 0.857

Structure W8UTR3

Pocket Pocket 1

P2Rank 0.991

Structure W8UTR3

Pocket Pocket 1

ColabFold model

FPocket 0.831 · Pocket 56

P2Rank 0.988 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 143 / 4744 genomes with a hit

Normalized 0.03

Sequence

Primary amino-acid sequence viewer.

MIPQISQAPGVVQLVLNFLQVLEQQGFTGDTATSYADRLTMATDNSVYQLLPDAVIFPRSTADVALLARVAAEPRFKSLIFTPRGGGTGTNGQALNGGIIVDMSRYMNRIIEINPDEGWVRVETGVIKDQLNQFLKPYGYFFAPELSTSNRATLGGMINTDASGQGSLVYGKTSDHVLGLRAVLMGGDILDTQAVPVALAETLGNTPSTVGRIYNTVYQRCKAQRDLIIDKFPKLNRFLTGYDLRHVFNDEMSEFDLTRILTGSEGTLAFITEARLDITRLPKVRRLVNVKYDSFDSALRNAPFMVEAKALSVETVDSKVLNLAREDIVWHSVSELITDVPDKEMLGLNIVEFAGDDAALIDQQVTTLCQRLDELMAASEAGVIGWQVCHDLEGVERIYAMRKKAVGLLGNAKGAAKPIPFAEDTCVPPEHLADYIVEFRALLDSHGLSYGMFGHVDAGVLHVRPALDMCDPQQEVLMKQISDDVVALTAKYGGLLWGEHGKGFRAEYSPAFFGETLYAELRKIKAVFDPDNRLNPGKICPPEGIDAPMMKVDAAKRGTWDRQIPIAVRSSWRGAMECNGNGLCFNFDVKSPMCPSMKVSNQRIHSPKGRATLVREWLRLLADRGVDPNQLEKALPEQGVSLRSLVARTRNSWHARKGEYDFSHEVKEAMSGCLACKACSTQCPIKIDVPEFRSRFLQLYHSRYLRPVRDHLVASVESYAPLMAQAPKTFNFFINQPWLKKLSEKHIGMVDLPLLSAPSLKQQMAGHRSANMTLEQLEALSAEQKAKMVLVVQDPFTSYYDAQVVADFIRLVEALGYQPVLLPFSPNGKAQHIKGFLTRFARTAQKTADFLNRVAQLGMPLVGVDPALVLCYRDEYKQTLGDKRGDFQVLLVHEWLPKALTSDARPDLGGEPWYLFGHCTEVTALPAATKQWADIFAHFGAKLENVSVGCCGMAGTYGHEVKNHANSLAIYALSWQQAMQRLPRNRCLVTGYSCRSQVKRIEGSGVRHPLQALLEIIG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1.1.99.39

Gene Ontology (GO)

GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
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: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:0051990 Catalysis of the reaction: (R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor.
GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0004458 Catalysis of the reaction: (R)-lactate + 2 [Fe(III)cytochrome c] = 2 [Fe(II)cytochrome c] + 2 H+ + pyruvate.
GO:0008720 Catalysis of the reaction: (R)-lactate + NAD+ = H+ + NADH + pyruvate.
GO:0046872 Binding to a metal ion.
GO:1903457 The chemical reactions and pathways resulting in the breakdown of lactate.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
516	691	SUPERFAMILY	SSF46548	alpha-helical ferredoxin
18	205	Gene3D	G3DSA:3.30.465.10	-
18	205	InterPro	IPR016169	FAD-binding, type PCMH, subdomain 2
673	684	ProSitePatterns	PS00198	4Fe-4S ferredoxin-type iron-sulfur binding region signature.
673	684	InterPro	IPR017900	4Fe-4S ferredoxin, iron-sulphur binding, conserved site
504	539	Gene3D	G3DSA:1.10.45.10	-
504	539	InterPro	IPR016171	Vanillyl-alcohol oxidase, C-terminal subdomain 2
48	281	ProSiteProfiles	PS51387	PCMH-type FAD-binding domain profile.
48	281	InterPro	IPR016166	FAD-binding domain, PCMH-type
52	192	Pfam	PF01565	FAD binding domain
52	192	InterPro	IPR006094	FAD linked oxidase, N-terminal
257	542	SUPERFAMILY	SSF55103	FAD-linked oxidases, C-terminal domain
257	542	InterPro	IPR016164	FAD-linked oxidase-like, C-terminal
13	543	PANTHER	PTHR11748	D-LACTATE DEHYDROGENASE
576	687	Pfam	PF13183	4Fe-4S dicluster domain
576	687	InterPro	IPR017896	4Fe-4S ferredoxin-type, iron-sulphur binding domain
662	695	ProSiteProfiles	PS51379	4Fe-4S ferredoxin-type iron-sulfur binding domain profile.
662	695	InterPro	IPR017896	4Fe-4S ferredoxin-type, iron-sulphur binding domain
420	500	Gene3D	G3DSA:3.30.70.2740	-
420	500	FunFam	G3DSA:3.30.70.2740:FF:000003	Oxidoreductase, FAD-binding, putative
281	539	Pfam	PF02913	FAD linked oxidases, C-terminal domain
281	539	InterPro	IPR004113	FAD-binding oxidoreductase/transferase, type 4, C-terminal
16	217	FunFam	G3DSA:3.30.465.10:FF:000024	Oxidoreductase, FAD-binding protein
21	282	SUPERFAMILY	SSF56176	FAD-binding/transporter-associated domain-like
21	282	InterPro	IPR036318	FAD-binding, type PCMH-like superfamily

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_W8UTR3	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_04654	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				0.857
4				0.853
29				0.229

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	38.72	0.96
2	36.02	0.954
3	13.31	0.681
4	9.39	0.504
5	6.04	0.298

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
56				0.831
3				0.796
1				0.368

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	36.83	0.956
2	33.45	0.947
3	15.17	0.747
4	8.46	0.452
5	4.83	0.215

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.

70 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
1DO	4BC7	P97275	186.3 Da LogP 3.90 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO`
2HG	6LPP	Q8N465	148.1 Da LogP -0.70 TPSA 94.8	✓ Ro5	✓ Clean	`C(CC(=O)O)[C@H](C(=O)O)O`
AKG	6LPX	Q8N465	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
AWB	5AE3	P97275	548.6 Da LogP 3.48 TPSA 157.3	1 viol.	✓ Clean	`CCCCCC[C@@H]1[C@H]([C@@H](OC(=O)[C@H]([C@H](OC1…`
B2Z	5AE1	P97275	341.4 Da LogP 3.37 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)N[C@H](C)c1ccc2c(c1)NC(=O)N2)c3cc…`
BEZ	5FXF	Q0SBK1	122.1 Da LogP 1.38 TPSA 37.3	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)O`
CIY	5FXE	Q0SBK1	178.2 Da LogP 1.61 TPSA 46.5	✓ Ro5	✓ Clean	`COc1cc(ccc1O)/C=C/C=O`
EPT	1AHZ	P56216	192.3 Da LogP 3.91 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCc1ccc(cc1)O`
EUG	1DZN	P56216	164.2 Da LogP 2.43 TPSA 29.5	✓ Ro5	✓ Clean	`C/C=C/c1ccc(c(c1)OC)O`
F6T	6GOU	P97275	345.3 Da LogP 2.94 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)NCc1ccc2c(c1)NC(=O)N2)c3c(cccc3F)F`
FAA	1AHU	P56216	891.7 Da LogP -2.41 TPSA 377.0	3 viol.	✓ Clean	`Cc1cc2c(cc1C)[N+](=C3C(=O)NC(=O)N=C3N2C[C@@H]([…`
FCR	1E0Y	P56216	162.1 Da LogP 2.41 TPSA 20.2	✓ Ro5	✓ Clean	`c1cc(ccc1C(F)(F)F)O`
FYC	5AE2	P97275	325.3 Da LogP 2.71 TPSA 77.8	✓ Ro5	✓ Clean	`C/C(=C\c1ccccc1F)/C(=O)NCc2ccc3c(c2)NC(=O)N3`
KQS	5ADZ	P97275	327.4 Da LogP 2.81 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)NCc1ccc2c(c1)NC(=O)N2)c3ccccc3F`
LAC	6LPT	Q8N465	90.1 Da LogP -0.55 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)O`
MLT	6LPQ	Q8N465	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
NCR	1AHV	P56216	153.1 Da LogP 1.61 TPSA 63.4	✓ Ro5	✓ Clean	`Cc1ccc(c(c1)[N+](=O)[O-])O`
S2G	6LPU	Q8N465	148.1 Da LogP -0.70 TPSA 94.8	✓ Ro5	✓ Clean	`C(CC(=O)O)[C@@H](C(=O)O)O`
V55	5FXP	Q0SBK1	152.1 Da LogP 1.21 TPSA 46.5	✓ Ro5	✓ Clean	`COc1cc(ccc1O)C=O`

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
CHEMBL4563407	O00116	—	345.3 Da LogP 2.94 TPSA 77.8	✓ Ro5	✓ Clean	`CC(CC(=O)NCc1ccc2[nH]c(=O)[nH]c2c1)c1c(F)cccc1F`

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
ZINC1644076	1.000	214.4 Da LogP 4.68 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCO`
ZINC1680803	1.000	200.4 Da LogP 4.29 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCO`
ZINC13840578	0.842	238.2 Da LogP 4.08 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1ccc(-c2ccc(C(F)(F)F)cc2)cc1`
ZINC26893796	0.840	240.3 Da LogP 4.79 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCc1ccc(-c2ccc(O)cc2)cc1`
ZINC3269660	0.824	254.2 Da LogP 2.45 TPSA 71.4	✓ Ro5	Alert	`O=C(O)c1ccc(C(=O)C(=O)c2ccccc2)cc1`
ZINC2504355	0.778	226.2 Da LogP 2.62 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)c2ccccc2)cc1`
ZINC1556080	0.773	256.3 Da LogP 4.05 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(CCCCCc2ccc(O)cc2)cc1`
ZINC1842893	0.773	270.4 Da LogP 4.44 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(CCCCCCc2ccc(O)cc2)cc1`
ZINC185070	0.733	272.3 Da LogP 3.29 TPSA 58.9	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2ccc(O)c(OC)c2)ccc1O`
ZINC26893690	0.731	226.3 Da LogP 4.40 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCc1ccc(-c2ccc(O)cc2)cc1`
ZINC56877	0.727	254.2 Da LogP 4.20 TPSA 29.5	✓ Ro5	✓ Clean	`Oc1ccc(Oc2ccc(C(F)(F)F)cc2)cc1`
ZINC100235123	0.692	248.4 Da LogP 4.51 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCc1ccc(CCO)cc1`
ZINC72400230	0.692	234.4 Da LogP 4.12 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCc1ccc(CCO)cc1`
ZINC85548070	0.692	220.4 Da LogP 4.08 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCc1ccc(CO)cc1`
ZINC1081124	0.688	214.1 Da LogP 3.72 TPSA 0.0	✓ Ro5	✓ Clean	`FC(F)(F)c1ccc(C(F)(F)F)cc1`
ZINC1672966	0.688	210.2 Da LogP 2.75 TPSA 34.1	✓ Ro5	Alert	`O=C(C(=O)c1ccccc1)c1ccccc1`
ZINC2149802	0.684	210.4 Da LogP 3.90 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCC#CCCCCCCO`
ZINC2529860	0.684	286.2 Da LogP 3.98 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(C(F)(F)C(F)(F)c2ccc(O)cc2)cc1`
ZINC2555300	0.684	238.4 Da LogP 4.68 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCC#CCCCCCCCCO`
ZINC2579260	0.684	238.4 Da LogP 4.68 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCC#CCCCCCCO`
ZINC34057267	0.684	274.3 Da LogP 4.72 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(-c3ccccc3)cc2)cc1`
ZINC59724910	0.684	212.4 Da LogP 4.46 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCO`
ZINC59724924	0.684	212.4 Da LogP 4.46 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCO`
ZINC59724927	0.684	212.4 Da LogP 4.46 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCO`
ZINC95831576	0.684	230.4 Da LogP 3.92 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCCCO`
ZINC1857579176	0.679	345.3 Da LogP 3.36 TPSA 78.0	✓ Ro5	✓ Clean	`C[C@H](CC(=O)NCc1ccc2nc(O)[nH]c2c1)c1c(F)cccc1F`
ZINC1857606065	0.679	345.3 Da LogP 3.36 TPSA 78.0	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)NCc1ccc2nc(O)[nH]c2c1)c1c(F)cccc1F`
ZINC71773889	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@H](O)C(=O)O`
ZINC71773890	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC71773891	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC1556073	0.652	228.3 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(CCCc2ccc(O)cc2)cc1`
ZINC114185151	0.647	298.2 Da LogP 2.15 TPSA 108.7	✓ Ro5	Alert	`O=C(O)c1ccc(C(=O)C(=O)c2ccc(C(=O)O)cc2)cc1`
ZINC13541228	0.647	258.3 Da LogP 2.98 TPSA 69.9	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2cc(O)cc(O)c2)ccc1O`
ZINC1590838	0.647	342.4 Da LogP 3.82 TPSA 68.3	✓ Ro5	Alert	`O=C(C(=O)c1ccc(C(=O)C(=O)c2ccccc2)cc1)c1ccccc1`
ZINC16133932	0.647	474.5 Da LogP 4.88 TPSA 102.4	✓ Ro5	Alert	`O=C(C(=O)c1ccc(C(=O)C(=O)c2ccc(C(=O)C(=O)c3cccc…`
ZINC2053487767	0.647	258.3 Da LogP 2.98 TPSA 69.9	✓ Ro5	✓ Clean	`COc1cc(C=Cc2cc(O)cc(O)c2)ccc1O`
ZINC1635826	0.645	300.3 Da LogP 2.57 TPSA 83.6	✓ Ro5	Alert	`COc1cc(/C=N/N=C/c2ccc(O)c(OC)c2)ccc1O`
ZINC16997495	0.645	300.3 Da LogP 2.57 TPSA 83.6	✓ Ro5	Alert	`COc1cc(/C=N\N=C/c2ccc(O)c(OC)c2)ccc1O`
ZINC254438868	0.645	300.3 Da LogP 2.57 TPSA 83.6	✓ Ro5	Alert	`COc1cc(C=NN=Cc2ccc(O)c(OC)c2)ccc1O`
ZINC5022931	0.645	300.3 Da LogP 2.57 TPSA 83.6	✓ Ro5	Alert	`COc1cc(/C=N\N=C\c2ccc(O)c(OC)c2)ccc1O`
ZINC100011055	0.630	302.2 Da LogP 4.80 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCCc1ccc(I)cc1`
ZINC1604287	0.630	205.3 Da LogP 3.31 TPSA 26.0	✓ Ro5	✓ Clean	`CCCCCCc1ccc(CCN)cc1`
ZINC2169753	0.630	241.2 Da LogP 4.57 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCc1ccc(Br)cc1`
ZINC2169754	0.630	255.2 Da LogP 4.96 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCCc1ccc(Br)cc1`
ZINC2390981	0.630	219.4 Da LogP 4.56 TPSA 26.0	✓ Ro5	Alert	`CCCCCCCCCc1ccc(N)cc1`
ZINC2524630	0.630	219.4 Da LogP 4.05 TPSA 26.0	✓ Ro5	✓ Clean	`CCCCCCCCc1ccc(CN)cc1`
ZINC2567977	0.630	233.4 Da LogP 4.95 TPSA 26.0	✓ Ro5	Alert	`CCCCCCCCCCc1ccc(N)cc1`
ZINC2567979	0.630	205.3 Da LogP 4.17 TPSA 26.0	✓ Ro5	Alert	`CCCCCCCCc1ccc(N)cc1`
ZINC72283205	0.630	288.2 Da LogP 4.41 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCc1ccc(I)cc1`
ZINC120595	0.629	226.3 Da LogP 3.57 TPSA 29.5	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2ccccc2)ccc1O`

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.