Protein target profile

KP13_04549

NAD-dependent malic enzyme

Genome: KpKP13 Gene: sfcA AHE44424.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTA5

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Length 565

Pocket druggability 0.636

Direct ligand evidence 0 65 total records

Functional annotation 1 EC 7 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.64. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.90. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 48.56 Lower values reduce human off-target concern.
Human E-value: 9.06e-81
Gut microbiome similarity: 2.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 42.435 Higher values support similarity to known essential genes.
DEG E-value: 8.77e-158 Smaller values mean stronger essential-gene similarity.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 95.19 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.636

Structure A0A0H3GTA5

Pocket Pocket 31

P2Rank 0.898

Structure A0A0H3GTA5

Pocket Pocket 1

ColabFold model

FPocket 0.899 · Pocket 25

P2Rank 0.896 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 128 / 4744 genomes with a hit

Prevalence 2.7%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GTA5

Chemistry

ChEMBL G9A ChEMBL MAE

Sequence

Primary amino-acid sequence viewer.

MQFTHKKNRSLYIPYAGPVLLEFPLLNKGSAFSMEERSNFNLLGLLPEVVETIEEQAERAWIQYQGFKTEIDKHIYLRNIQDTNETLFYRLIGNHLEEMMPVIYTPTVGAACERFSEIYRRARGVFISYQNRHNLDDILQNVPNHNVKVIVVTDGERILGLGDQGIGGMGIPIGKLSLYTTCGGISPAYTLPIVLDVGTNNQQLLDDPLYMGWRHPRITDDEYYQFVDDVIQAIKARWPDVLLQFEDFAQKNAMPLLNRYRNEICSFNDDIQGTAAVTVGTLIAASRGAGSQLSEQKIVFLGAGSAGCGIAEQIIAQIVREGLSEEEARQRVFMVDRFGLLTDGMPNLLPFQNKLVQKREQLQSWDTTSEALSLLDVVRNVKPNILIGVSGQPGLFTEEIIREMHKHCPRPIVMPLSNPTSRVEATPQNILSWTDGEALVATGSPFSPVTVKGKQYPIAQCNNSYIFPGIGLGVIASGASRVTDEMLMAASETLAQHSPLVNNGEGPVLPELKDIQTVSRAIAFAVGKVAQEQGVAVKTSAEALLQAISDNFWLPEYRNYRRTSI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1.1.1.38

Gene Ontology (GO)

GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0004470 Catalysis of the oxidative decarboxylation of malate with the concomitant production of pyruvate.
GO:0004471 Catalysis of the reaction: (S)-malate + NAD+ = pyruvate + CO2 + NADH.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046872 Binding to a metal ion.
GO:0008948 Catalysis of the reaction: H+ + oxaloacetate = CO2 + pyruvate.
GO:0006108 The chemical reactions and pathways involving malate, the anion of hydroxybutanedioic acid, a chiral hydroxydicarboxylic acid. The (+) enantiomer is an important intermediate in metabolism as a component of both the TCA cycle and the glyoxylate cycle.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
81	261	SMART	SM01274	malic_2
81	261	InterPro	IPR012301	Malic enzyme, N-terminal domain
16	268	FunFam	G3DSA:3.40.50.10380:FF:000001	NAD-dependent malic enzyme
81	261	Pfam	PF00390	Malic enzyme, N-terminal domain
271	562	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
271	562	InterPro	IPR036291	NAD(P)-binding domain superfamily
5	270	SUPERFAMILY	SSF53223	Aminoacid dehydrogenase-like, N-terminal domain
5	270	InterPro	IPR046346	Aminoacid dehydrogenase-like, N-terminal domain superfamily
4	565	Hamap	MF_01619	NAD-dependent malic enzyme [maeA].
4	565	InterPro	IPR023667	NAD-dependent malic enzyme, proteobacteria
2	563	PIRSF	PIRSF000106	ME
2	563	InterPro	IPR001891	Malic oxidoreductase
271	531	SMART	SM00919	Malic_M_2
271	531	InterPro	IPR012302	Malic enzyme, NAD-binding
271	555	CDD	cd05312	NAD_bind_1_malic_enz
14	560	PANTHER	PTHR23406	MALIC ENZYME-RELATED
271	530	Pfam	PF03949	Malic enzyme, NAD binding domain
271	530	InterPro	IPR012302	Malic enzyme, NAD-binding
269	564	FunFam	G3DSA:3.40.50.720:FF:000055	NAD-dependent malic enzyme
16	268	Gene3D	G3DSA:3.40.50.10380	-
16	268	InterPro	IPR037062	Malic enzyme, N-terminal domain superfamily
269	564	Gene3D	G3DSA:3.40.50.720	-
267	283	PRINTS	PR00072	Malic enzyme signature
267	283	InterPro	IPR001891	Malic oxidoreductase
87	111	PRINTS	PR00072	Malic enzyme signature
87	111	InterPro	IPR001891	Malic oxidoreductase
183	205	PRINTS	PR00072	Malic enzyme signature
183	205	InterPro	IPR001891	Malic oxidoreductase
408	424	PRINTS	PR00072	Malic enzyme signature
408	424	InterPro	IPR001891	Malic oxidoreductase
147	176	PRINTS	PR00072	Malic enzyme signature
147	176	InterPro	IPR001891	Malic oxidoreductase
298	314	PRINTS	PR00072	Malic enzyme signature
298	314	InterPro	IPR001891	Malic oxidoreductase
242	260	PRINTS	PR00072	Malic enzyme signature
242	260	InterPro	IPR001891	Malic oxidoreductase
267	283	ProSitePatterns	PS00331	Malic enzymes signature.
267	283	InterPro	IPR015884	Malic enzyme, conserved site

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #31

0.636

Likely same site as P2Rank 1 2.9 Å 25 shared residues 89% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #1

0.565

Likely same site as P2Rank 4 0.9 Å 14 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.898

Likely same site as FPocket 31 2.9 Å 25 shared residues 89% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.372

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Surrounding area

Site 3 P2Rank #3

0.334

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Surrounding area

Site 4 P2Rank #4

0.276

Likely same site as FPocket 1 0.9 Å 14 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.188

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Surrounding area

Residue sets

UniProt: Active site:104-104 Proton donor

UniProt: Active site:175-175 Proton acceptor

UniProt: Binding site:157-157

UniProt: Binding site:246-246

UniProt: Binding site:247-247

UniProt: Binding site:270-270

UniProt: Binding site:418-418

UniProt: Binding site:462-462

UniProt: Site:270-270 Important for activity

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #25

0.899

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Surrounding area

Site 2 FPocket #2

0.76

Likely same site as P2Rank 1 4.5 Å 17 shared residues 77% of smaller site

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Surrounding area

Site 3 FPocket #1

0.495

Likely same site as P2Rank 2 1.5 Å 15 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.896

Likely same site as FPocket 2 4.5 Å 17 shared residues 77% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.414

Likely same site as FPocket 1 1.5 Å 15 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.365

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Surrounding area

Site 4 P2Rank #4

0.289

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Surrounding area

Site 5 P2Rank #5

0.234

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GTA5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04549	ColabFold	—	—	full sequence	—	Loaded

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.

65 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 15 records from similar proteins

Structural ligands 13 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

FUM PDB via homolog 116.1 Da · LogP -0.29 · TPSA 74.6 Open detail RCSB PDB

MAK PDB via homolog Detail RCSB PDB

MLT PDB via homolog Detail RCSB PDB

OXL PDB via homolog Detail RCSB PDB

PYR PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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
FUM RCSB PDB	1GZ3	P23368	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
MAK RCSB PDB	1EFK	P23368	118.0 Da LogP -1.28 TPSA 91.7	✓ Ro5	✓ Clean	`C(=O)(C(=O)O)C(=O)O`
MLT RCSB PDB	1PJ4	P23368	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
OXL RCSB PDB	1DO8	P23368	88.0 Da LogP -3.51 TPSA 80.3	✓ Ro5	✓ Clean	`C(=O)(C(=O)[O-])[O-]`
PYR RCSB PDB	1PJ3	P23368	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
SEV RCSB PDB	6W29	Q4DJ68	418.4 Da LogP 4.03 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(cc1)NS(=O)(=O)c2cccc(c2)NC(=O)c3cc(cc(c…`
SJD RCSB PDB	6W2N	Q4DJ68	436.4 Da LogP 4.17 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(c(c1)F)NS(=O)(=O)c2cccc(c2)NC(=O)c3cc(c…`
SWV RCSB PDB	6W49	Q4DJ68	372.4 Da LogP 2.67 TPSA 101.1	✓ Ro5	✓ Clean	`c1ccc(c(c1)NS(=O)(=O)c2cccc(c2)NC(=O)c3cnccn3)F`
SZD RCSB PDB	6W59	Q4DJ68	472.4 Da LogP 4.92 TPSA 84.5	✓ Ro5	✓ Clean	`c1cc(cc(c1)S(=O)(=O)Nc2ccc(cc2)OC(F)(F)F)NC(=O)…`
SZG RCSB PDB	6W57	Q4DJ68	488.8 Da LogP 5.27 TPSA 84.5	1 viol.	✓ Clean	`c1cc(ccc1NS(=O)(=O)c2ccc(c(c2)NC(=O)c3cc(cc(c3)…`
SZJ RCSB PDB	6W56	Q4DJ68	454.4 Da LogP 4.62 TPSA 84.5	✓ Ro5	✓ Clean	`c1cc(cc(c1)S(=O)(=O)Nc2ccc(cc2)OC(F)F)NC(=O)c3c…`
SZP RCSB PDB	6W53	Q4DJ68	506.8 Da LogP 5.57 TPSA 84.5	2 viol.	✓ Clean	`c1cc(ccc1NS(=O)(=O)c2ccc(c(c2)NC(=O)c3cc(cc(c3)…`
TTN RCSB PDB	1O0S	P27443	118.0 Da LogP -4.15 TPSA 100.5	✓ Ro5	✓ Clean	`C(C(=O)[O-])(C(=O)[O-])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
G9A ChEMBL	Q16798	—	130.1 Da LogP 0.10 TPSA 74.6	✓ Ro5	✓ Clean	`C(/C=C/C(=O)O)C(=O)O`
MAE ChEMBL	Q16798	—	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)/C(=O)O`

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
ZINC8289540 ZINC	0.809	412.5 Da LogP 3.76 TPSA 93.7	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3ccc(OC)cc3)c2)…`
ZINC9217064 ZINC	0.792	388.8 Da LogP 3.18 TPSA 101.0	✓ Ro5	✓ Clean	`O=C(Nc1cccc(S(=O)(=O)Nc2ccccc2Cl)c1)c1cnccn1`
ZINC8287843 ZINC	0.784	400.4 Da LogP 3.89 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(C(=O)Nc3cccc(F)c3)c2)c…`
ZINC5864247 ZINC	0.776	382.4 Da LogP 3.75 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3ccccc3)c2)cc1`
ZINC8289545 ZINC	0.760	412.5 Da LogP 3.76 TPSA 93.7	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3cccc(OC)c3)c2)…`
ZINC12532621 ZINC	0.759	466.4 Da LogP 4.65 TPSA 93.7	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3ccc(OC(F)(F)F)…`
ZINC12552275 ZINC	0.745	418.4 Da LogP 4.03 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccccc1NS(=O)(=O)c1cccc(NC(=O)c2cc(F)cc(F)c2…`
ZINC68732608 ZINC	0.745	400.4 Da LogP 3.89 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)c2ccc(NS(=O)(=O)c3cccc(F)c3)cc2)c…`
ZINC89444372 ZINC	0.745	400.4 Da LogP 3.89 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)c2cccc(S(=O)(=O)Nc3ccc(F)cc3)c2)c…`
ZINC9715810 ZINC	0.736	450.4 Da LogP 4.77 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3ccc(C(F)(F)F)c…`
ZINC5557605 ZINC	0.725	415.4 Da LogP 4.28 TPSA 96.5	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)Nc3ccc(F)cc3)c2)…`
ZINC10027204 ZINC	0.722	388.8 Da LogP 3.18 TPSA 101.0	✓ Ro5	✓ Clean	`O=C(Nc1cccc(S(=O)(=O)Nc2ccc(Cl)cc2)c1)c1cnccn1`
ZINC8129611 ZINC	0.717	371.4 Da LogP 3.27 TPSA 88.2	✓ Ro5	✓ Clean	`O=C(Nc1cccc(S(=O)(=O)Nc2ccccc2F)c1)c1ccncc1`
ZINC3014061 ZINC	0.714	412.5 Da LogP 3.76 TPSA 93.7	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)c2cccc(S(=O)(=O)Nc3ccc(OC)cc3)c2)…`
ZINC823266 ZINC	0.706	382.4 Da LogP 3.75 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(C(=O)Nc3ccccc3)c2)cc1`
ZINC6046379 ZINC	0.702	400.4 Da LogP 3.89 TPSA 84.5	✓ Ro5	✓ Clean	`COc1cccc(C(=O)Nc2cccc(S(=O)(=O)Nc3ccccc3F)c2)c1`
ZINC1532902 ZINC	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 ZINC	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`
ZINC754833 ZINC	0.698	426.5 Da LogP 3.45 TPSA 121.8	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(C(=O)Nc3cccc(C(=O)O)c3…`
ZINC89651324 ZINC	0.698	432.4 Da LogP 4.33 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cc(NC(=O)c3cc(F)cc(F)c3)ccc…`
ZINC1104233 ZINC	0.679	400.4 Da LogP 3.89 TPSA 84.5	✓ Ro5	✓ Clean	`COc1cccc(S(=O)(=O)Nc2ccc(C(=O)Nc3ccc(F)cc3)cc2)…`
ZINC12507851 ZINC	0.679	422.5 Da LogP 4.24 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3ccc4c(c3)CCC4)…`
ZINC12556970 ZINC	0.679	448.4 Da LogP 4.35 TPSA 93.7	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(C(=O)Nc3ccc(OC(F)F)cc3…`
ZINC27496348 ZINC	0.673	414.5 Da LogP 3.82 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)Cc3ccc(F)cc3)c2)…`
ZINC12541977 ZINC	0.667	447.5 Da LogP 4.54 TPSA 89.4	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3cccc(-n4cccc4)…`
ZINC5652634 ZINC	0.667	388.5 Da LogP 3.81 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3cccs3)c2)cc1`
ZINC6244639 ZINC	0.667	371.4 Da LogP 3.27 TPSA 88.2	✓ Ro5	✓ Clean	`O=C(Nc1cccnc1)c1cccc(S(=O)(=O)Nc2ccccc2F)c1`
ZINC6510588 ZINC	0.667	317.2 Da LogP 4.12 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(Nc1ccc(OC(F)(F)F)cc1)c1cc(F)cc(F)c1`
ZINC71773889 ZINC	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 ZINC	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 ZINC	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`
ZINC9612539 ZINC	0.667	417.9 Da LogP 3.80 TPSA 97.4	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3ccc(Cl)nc3)c2)…`
ZINC21875823 ZINC	0.660	418.4 Da LogP 4.34 TPSA 84.5	✓ Ro5	✓ Clean	`O=C(Nc1ccc(OC(F)F)cc1)c1ccc(NS(=O)(=O)c2ccccc2)…`
ZINC21877086 ZINC	0.660	436.4 Da LogP 4.64 TPSA 84.5	✓ Ro5	✓ Clean	`O=C(Nc1ccc(OC(F)(F)F)cc1)c1ccc(NS(=O)(=O)c2cccc…`
ZINC3329693 ZINC	0.660	341.3 Da LogP 3.29 TPSA 72.5	✓ Ro5	✓ Clean	`CC(=O)c1cccc(S(=O)(=O)Nc2ccc(OC(F)F)cc2)c1`
ZINC7055979 ZINC	0.660	359.3 Da LogP 3.59 TPSA 72.5	✓ Ro5	✓ Clean	`CC(=O)c1cccc(S(=O)(=O)Nc2ccc(OC(F)(F)F)cc2)c1`
ZINC7055973 ZINC	0.660	335.3 Da LogP 3.53 TPSA 55.4	✓ Ro5	✓ Clean	`O=S(=O)(Nc1ccc(OC(F)(F)F)cc1)c1cccc(F)c1`
ZINC7409087 ZINC	0.660	317.3 Da LogP 3.23 TPSA 55.4	✓ Ro5	✓ Clean	`O=S(=O)(Nc1ccc(OC(F)F)cc1)c1cccc(F)c1`
ZINC12739009 ZINC	0.655	375.4 Da LogP 3.18 TPSA 101.3	✓ Ro5	✓ Clean	`Cc1cc(C(=O)Nc2cccc(S(=O)(=O)Nc3ccccc3F)c2)no1`
ZINC89453684 ZINC	0.655	456.5 Da LogP 4.24 TPSA 101.6	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)CCC(=O)c3ccc(F)c…`
ZINC9217066 ZINC	0.655	426.5 Da LogP 3.48 TPSA 103.0	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3ccc4c(c3)OCO4)…`
ZINC9514424 ZINC	0.655	491.5 Da LogP 4.59 TPSA 126.7	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3ccc(NC(=O)c4cc…`
ZINC5881828 ZINC	0.655	383.4 Da LogP 3.14 TPSA 97.4	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2cccc(NC(=O)c3ccccn3)c2)cc1`
ZINC6046622 ZINC	0.655	416.9 Da LogP 4.40 TPSA 84.5	✓ Ro5	✓ Clean	`COc1cccc(C(=O)Nc2cccc(S(=O)(=O)Nc3ccc(Cl)cc3)c2…`
ZINC2635861 ZINC	0.654	361.3 Da LogP 3.08 TPSA 92.7	✓ Ro5	✓ Clean	`O=C(O)c1cccc(S(=O)(=O)Nc2ccc(OC(F)(F)F)cc2)c1`
ZINC3452732 ZINC	0.652	263.2 Da LogP 3.23 TPSA 38.3	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)c2cc(F)cc(F)c2)cc1`
ZINC3593496 ZINC	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 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC3154686 ZINC	0.648	426.5 Da LogP 3.45 TPSA 121.8	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)c2cccc(S(=O)(=O)Nc3ccc(C(=O)O)cc3…`
ZINC89444368 ZINC	0.648	416.9 Da LogP 4.40 TPSA 84.5	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)c2cccc(S(=O)(=O)Nc3ccc(Cl)cc3)c2)…`

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.