Protein target profile

VK055_0988

fumarate hydratase, class II

Genome: KpATCC43816 Gene: fumC AIK79612.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GWS1

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Length 456

Pocket druggability 0.806

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 59 total records

Functional annotation 1 EC 9 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

Central metabolic position More central than 99.1% of genes in this genome. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.81. This is a computational pocket signal, not binding validation. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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 (%): 61.858 Lower values reduce human off-target concern.
Human E-value: 2.48e-175
Gut microbiome similarity: 19.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 61.674 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 97.34 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 0.806

Structure A0A0H3GWS1

Pocket Pocket 5

P2Rank 0.124

Structure A0A0H3GWS1

Pocket Pocket 1

ColabFold model

FPocket 0.668 · Pocket 14

P2Rank 0.336 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 939 / 4744 genomes with a hit

Prevalence 19.8%

Cross-references

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

Sequence

UniProt A0A0H3GWS1

Pathways

KEGG R01082 BioCyc FUMHYDR-RXN

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: more central than 99.1% of genes in this genome.

Relative network centrality 99.1% more central than 99.1% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAGKHAQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALIALREKVIPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHIEASQPHLAELALGGTAVGTGLNTHPEYAVRVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGKVNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERISQLLNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEEMVGSLAIR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

4.2.1.2

Gene Ontology (GO)

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:0006106 The chemical reactions and pathways involving fumarate, the anion of trans-1,2-ethenedicarboxylic acid, the diastereoisomer of maleate. It is a key intermediate in metabolism and is formed in the TCA cycle from succinate and converted into malate.
GO:0045239 Any of the heteromeric enzymes that act in the TCA cycle.
GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
GO:0004333 Catalysis of the reaction: (S)-malate = fumarate + H2O.
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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0042802 Binding to an identical protein or proteins.
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.

30 records

Show feature table

Start	End	DB	Term	Name
398	450	Pfam	PF10415	Fumarase C C-terminus
398	450	InterPro	IPR018951	Fumarase C, C-terminal
398	454	Gene3D	G3DSA:1.10.40.30	-
1	451	PANTHER	PTHR11444	ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
1	451	InterPro	IPR005677	Fumarate hydratase, class II
170	188	PRINTS	PR00149	Fumarate lyase superfamily signature
170	188	InterPro	IPR000362	Fumarate lyase family
307	323	PRINTS	PR00149	Fumarate lyase superfamily signature
307	323	InterPro	IPR000362	Fumarate lyase family
261	288	PRINTS	PR00149	Fumarate lyase superfamily signature
261	288	InterPro	IPR000362	Fumarate lyase family
124	142	PRINTS	PR00149	Fumarate lyase superfamily signature
124	142	InterPro	IPR000362	Fumarate lyase family
397	454	FunFam	G3DSA:1.10.40.30:FF:000002	Fumarate hydratase class II
129	396	FunFam	G3DSA:1.20.200.10:FF:000001	Fumarate hydratase, mitochondrial
1	451	NCBIfam	TIGR00979	class II fumarate hydratase
1	449	SUPERFAMILY	SSF48557	L-aspartase-like
1	449	InterPro	IPR008948	L-Aspartase-like
129	397	Gene3D	G3DSA:1.20.200.10	Fumarase/aspartase (Central domain)
1	452	Hamap	MF_00743	Fumarate hydratase class II [fumC].
1	452	InterPro	IPR005677	Fumarate hydratase, class II
1	128	Gene3D	G3DSA:1.10.275.10	-
1	128	InterPro	IPR024083	Fumarase/histidase, N-terminal
2	332	Pfam	PF00206	Lyase
2	332	InterPro	IPR022761	Fumarate lyase, N-terminal
1	449	CDD	cd01362	Fumarase_classII
1	449	InterPro	IPR005677	Fumarate hydratase, class II
1	128	FunFam	G3DSA:1.10.275.10:FF:000001	Fumarate hydratase, mitochondrial
307	316	ProSitePatterns	PS00163	Fumarate lyases signature.
307	316	InterPro	IPR020557	Fumarate lyase, 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 #5

0.806

Likely same site as P2Rank 3 5.0 Å 9 shared residues 82% 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

0.124

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Surrounding area

Site 2 P2Rank #2

0.043

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Surrounding area

Site 3 P2Rank #3

0.035

Likely same site as FPocket 5 5.0 Å 9 shared residues 82% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.01

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Surrounding area

Site 5 P2Rank #5

0.006

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Surrounding area

Residue sets

UniProt: Active site:188-188 Proton donor/acceptor

UniProt: Active site:318-318

UniProt: Binding site:129-132 in site B

UniProt: Binding site:139-141

UniProt: Binding site:187-187

UniProt: Binding site:319-319

UniProt: Binding site:324-326

UniProt: Binding site:98-100

UniProt: Site:331-331 Important for catalytic activity

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.336

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Surrounding area

Site 2 P2Rank #2

0.021

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Surrounding area

Site 3 P2Rank #3

0.021

Likely same site as FPocket 14 6.1 Å 6 shared residues 67% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.012

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Surrounding area

Residue sets

UniProt: Active site:188-188 Proton donor/acceptor

UniProt: Active site:318-318

UniProt: Binding site:129-132 in site B

UniProt: Binding site:139-141

UniProt: Binding site:187-187

UniProt: Binding site:319-319

UniProt: Binding site:324-326

UniProt: Binding site:98-100

UniProt: Site:331-331 Important for catalytic activity

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_A0A0H3GWS1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0988	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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

APO PDB via homolog 169.1 Da · LogP -1.42 · TPSA 120.8 Open detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

FUM PDB via homolog Detail RCSB PDB

LMR PDB via homolog Detail RCSB PDB

MLI 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
APO RCSB PDB	7LUB	P07954	169.1 Da LogP -1.42 TPSA 120.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)N)P(=O)(O)O`
FLC RCSB PDB	6P3C	P05042	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
FUM RCSB PDB	7C18	Q65UJ3	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
LMR RCSB PDB	6U4O	A0A3Q0KQY7	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)O)C(=O)O`
MLI RCSB PDB	3GTD	Q9ZCQ4	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MLT RCSB PDB	1FUO	P05042	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
PMA RCSB PDB	1FUP	P05042	254.1 Da LogP 0.48 TPSA 149.2	✓ Ro5	✓ Clean	`c1c(c(cc(c1C(=O)O)C(=O)O)C(=O)O)C(=O)O`
SIF RCSB PDB	1FUQ	P05042	190.3 Da LogP 1.25 TPSA 74.6	✓ Ro5	✓ Clean	`C[Si](C)(C)C(CC(=O)O)C(=O)O`
TLA RCSB PDB	6VBE	P07954	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)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).

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
ZINC391925 ZINC	1.000	254.1 Da LogP 0.48 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)O)cc1C(=O)O`
ZINC22204540 ZINC	0.800	446.3 Da LogP 1.11 TPSA 240.9	1 viol.	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)c2cc(C(=O)O)c(C(=O)O)c…`
ZINC4289585 ZINC	0.706	226.1 Da LogP 0.49 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)O)cc1O`
ZINC4863098 ZINC	0.706	250.2 Da LogP 1.49 TPSA 108.7	✓ Ro5	✓ Clean	`CC(=O)c1cc(C(=O)O)c(C(C)=O)cc1C(=O)O`
ZINC95938319 ZINC	0.706	252.2 Da LogP 0.85 TPSA 162.8	1 viol.	✓ Clean	`N=C(O)c1cc(C(=N)O)c(C(=O)O)cc1C(=O)O`
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`
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC225924 ZINC	0.667	330.2 Da LogP 2.15 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(C(=O)O)c(C(=O)O)c2)cc1C(=O)O`
ZINC391804 ZINC	0.667	216.2 Da LogP 2.24 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cc2ccccc2cc1C(=O)O`
ZINC4553176 ZINC	0.667	289.0 Da LogP 1.54 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)O)cc1Br`
ZINC59202638 ZINC	0.667	244.6 Da LogP 1.43 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)O)cc1Cl`
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`
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`
ZINC20357711 ZINC	0.647	323.9 Da LogP 2.61 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cc(Br)c(Br)cc1C(=O)O`
ZINC346796 ZINC	0.647	202.1 Da LogP 1.36 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cc(F)c(F)cc1C(=O)O`
ZINC4428360 ZINC	0.647	298.2 Da LogP 0.18 TPSA 186.5	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)O)c(C(=O)O)c1C(=O)O`
ZINC56485 ZINC	0.647	235.0 Da LogP 2.39 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cc(Cl)c(Cl)cc1C(=O)O`
ZINC105301 ZINC	0.632	210.1 Da LogP 0.78 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)O)c(C(=O)O)c1`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC388195 ZINC	0.625	304.2 Da LogP 1.63 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)O)c2c(C(=O)O)ccc(C(=O)O)c12`
ZINC25490549 ZINC	0.611	323.9 Da LogP 2.61 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(Br)cc1Br`
ZINC642881320 ZINC	0.611	378.3 Da LogP 3.38 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c2ccc3c(C(=O)O)cc(C(=O)O)c4cc…`
ZINC75852200 ZINC	0.611	220.1 Da LogP 1.50 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(F)c(F)c1F`
ZINC133154 ZINC	0.600	200.6 Da LogP 1.74 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(Cl)cc1C(=O)O`
ZINC1571173 ZINC	0.600	245.0 Da LogP 1.85 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(Br)cc1C(=O)O`
ZINC1675303 ZINC	0.600	292.0 Da LogP 1.69 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(I)cc1C(=O)O`
ZINC1995075 ZINC	0.600	358.3 Da LogP 1.71 TPSA 166.3	✓ Ro5	✓ Clean	`O=C(c1ccc(C(=O)O)c(C(=O)O)c1)c1ccc(C(=O)O)c(C(=…`
ZINC39205416 ZINC	0.600	266.3 Da LogP 3.39 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc3ccccc3cc2cc1C(=O)O`
ZINC44069231 ZINC	0.600	314.2 Da LogP 2.01 TPSA 129.0	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)c2ccccc2)cc1C(=O)O`
ZINC1560405156 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC2040496 ZINC	0.588	254.1 Da LogP 0.48 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)O)c(C(=O)O)c1C(=O)O`
ZINC3120959 ZINC	0.579	255.1 Da LogP -0.13 TPSA 162.1	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)O)nc1C(=O)O`
ZINC81217827 ZINC	0.579	222.2 Da LogP 2.21 TPSA 74.6	✓ Ro5	✓ Clean	`CCc1cc(C(=O)O)c(C(=O)O)cc1CC`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC100725222 ZINC	0.571	358.3 Da LogP 2.89 TPSA 173.9	✓ Ro5	Alert	`O=C(O)c1ccc(/N=N/c2ccc(C(=O)O)c(C(=O)O)c2)cc1C(…`
ZINC66325523 ZINC	0.571	290.2 Da LogP 0.03 TPSA 166.3	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(S(=O)(=O)O)cc1C(=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.