KpATCC43816 Protein target profile

quinolinate synthetase complex, A subunit

Accession: VK055_1772

Gene: AIK80392.1 nadA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GU73

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Length 347

Pocket druggability (P2Rank · AlphaFold DB model) 0.889

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 72 total records

Functional annotation 1 EC 7 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 95.9% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. 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: No hit
Gut microbiome similarity: 3.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 70.303 Higher values support similarity to known essential genes.
DEG E-value: 3.03e-176 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 93.32 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.889

Structure A0A0H3GU73

Pocket Pocket 1

Druggability (FPocket) 0.87

Structure A0A0H3GU73

Pocket Pocket 17

ColabFold model

P2Rank 0.911 · Pocket 1

FPocket 0.945 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 163 / 4744 genomes with a hit

Prevalence 3.4%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Nicotinate and nicotinamide metabolism, no isoenzyme backup detected, more central than 95.9% of genes in this genome, no human homolog detected.

Relative network centrality 95.9% more central than 95.9% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSVMFDPETAIYPFPAKPQPLTVDEKQFYREKIKRLLRERDAVMVAHYYTDPEIQQLAEETGGCIADSLEMARFGARHSASTLLVAGVRFMGETAKILSPEKTILMPTLNAECSLDLGCPIEEFNAFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIDHLDSLGQKILWAPDRHLGRYVQRQTGADVLCWQGACIVHDEFKTQALMRMKALHPEAAVLVHPESPQAIVEMADAVGSTSQLIAAAKSLPQRQLIVATDRGIFYKMQQAVPEKTLLEAPTAGEGATCRSCAHCPWMAMNGLKAIAEGLEQGGAEHEIHVDEALRTGALIPLNRMLDFAATLRG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.5.1.72

Gene Ontology (GO)

GO:0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (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:0009435 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions. NAD+ is derived from various sources including vitamin B3.
GO:0008987 Catalysis of the reaction: iminoaspartate + dihydroxy-acetone-phosphate = quinolinate + 2 H2O + phosphate.
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:0034628 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), beginning with the catabolism of L-aspartate into the precursor quinolinate. NAD+ is a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
285	344	PANTHER	PTHR30573	QUINOLINATE SYNTHETASE A
285	344	InterPro	IPR003473	Quinolinate synthetase A
200	295	Gene3D	G3DSA:3.40.50.10800	-
200	295	InterPro	IPR036094	Quinolinate synthetase A superfamily
115	215	FunFam	G3DSA:3.40.50.10800:FF:000003	Quinolinate synthase A
27	341	NCBIfam	TIGR00550	quinolinate synthase
27	341	InterPro	IPR003473	Quinolinate synthetase A
29	341	SUPERFAMILY	SSF142754	NadA-like
29	341	InterPro	IPR036094	Quinolinate synthetase A superfamily
32	322	Gene3D	G3DSA:3.40.50.10800	-
32	322	InterPro	IPR036094	Quinolinate synthetase A superfamily
1	347	Hamap	MF_00567	Quinolinate synthase [nadA].
1	347	InterPro	IPR023513	Quinolinate synthase A, type 1
115	339	Gene3D	G3DSA:3.40.50.10800	-
115	339	InterPro	IPR036094	Quinolinate synthetase A superfamily
31	340	Pfam	PF02445	Quinolinate synthetase A protein
31	340	InterPro	IPR003473	Quinolinate synthetase A

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.889

Likely same site as FPocket 2 0.8 Å 19 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.072

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Surrounding area

Pocket 3 P2Rank #3

0.052

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Surrounding area

Pocket 4 P2Rank #4

0.037

Likely same site as FPocket 17 1.9 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.031

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #17

0.87 Unusual size

Likely same site as P2Rank 4 1.9 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #2

0.632

Likely same site as P2Rank 1 0.8 Å 19 shared residues 100% of smaller site

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Surrounding area

Pocket 3 FPocket #1

0.28

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Surrounding area

Residue sets

UniProt: Binding site:114-114

UniProt: Binding site:140-142

UniProt: Binding site:157-157

UniProt: Binding site:201-201

UniProt: Binding site:227-229

UniProt: Binding site:244-244

UniProt: Binding site:298-298

UniProt: Binding site:48-48

UniProt: Binding site:69-69

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.911

Likely same site as FPocket 1 4.2 Å 23 shared residues 96% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.085

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Surrounding area

Pocket 3 P2Rank #3

0.064

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Surrounding area

Pocket 4 P2Rank #4

0.045

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Surrounding area

Pocket 5 P2Rank #5

0.015

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.945 Unusual size

Likely same site as P2Rank 1 4.2 Å 23 shared residues 96% of smaller site

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Surrounding area

Pocket 2 FPocket #4

0.515

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Surrounding area

Residue sets

UniProt: Binding site:114-114

UniProt: Binding site:140-142

UniProt: Binding site:157-157

UniProt: Binding site:201-201

UniProt: Binding site:227-229

UniProt: Binding site:244-244

UniProt: Binding site:298-298

UniProt: Binding site:48-48

UniProt: Binding site:69-69

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_A0A0H3GU73	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1772	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.

72 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 22 records from similar proteins

Structural ligands 22 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

13P PDB via homolog 170.1 Da · LogP -1.34 · TPSA 104.1 Open detail RCSB PDB

5UK PDB via homolog Detail RCSB PDB

5XR PDB via homolog Detail RCSB PDB

5XW PDB via homolog Detail RCSB PDB

CIZ 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
13P RCSB PDB	5KTN	O57767	170.1 Da LogP -1.34 TPSA 104.1	✓ Ro5	✓ Clean	`C(C(=O)COP(=O)(O)O)O`
5UK RCSB PDB	5F3D	Q9X1X7	203.1 Da LogP -1.26 TPSA 135.8	✓ Ro5	✓ Clean	`[H]/N=C(\[C@H](CC(=O)CO)C(=O)O)/C(=O)O`
5XR RCSB PDB	6OR8	O57767	221.2 Da LogP -2.27 TPSA 144.2	✓ Ro5	✓ Clean	`C(C=O)[C@@H](N[C@@](CC(=O)O)(C(=O)O)O)O`
5XW RCSB PDB	6ORA	O57767	203.2 Da LogP -1.11 TPSA 124.3	✓ Ro5	✓ Clean	`C(C=O)C(/N=C(/CC(=O)O)\C(=O)O)O`
CIZ RCSB PDB	5KTS	O57767	130.1 Da LogP 0.10 TPSA 74.6	✓ Ro5	✓ Clean	`C/C(=C/C(=O)O)/C(=O)O`
DYA RCSB PDB	6NSU	O57767	131.1 Da LogP -1.00 TPSA 100.6	✓ Ro5	✓ Clean	`C(=C(/C(=O)O)\N)\C(=O)O`
FLC RCSB PDB	5F35	Q9X1X7	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
GZ8 RCSB PDB	6I0K	Q9X1X7	198.2 Da LogP 0.64 TPSA 74.6	✓ Ro5	Alert	`C1=CC(=S)C=C(C1C(=O)O)C(=O)O`
H2S RCSB PDB	6I0R	Q9X1X7	34.1 Da LogP 0.11 TPSA 0.0	✓ Ro5	✓ Clean	`S`
ITN RCSB PDB	5KTP	O57767	130.1 Da LogP 0.10 TPSA 74.6	✓ Ro5	✓ Clean	`C=C(CC(=O)O)C(=O)O`
LMR RCSB PDB	5KTT	O57767	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)O)C(=O)O`
MAE RCSB PDB	5KTR	O57767	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)/C(=O)O`
MLT RCSB PDB	1WZU	O57767	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
NH4 RCSB PDB	5KTN	O57767	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
NHE RCSB PDB	6F4L	Q9X1X7	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=O)(=O)O`
NTM RCSB PDB	5LQS	Q9X1X7	167.1 Da LogP 0.48 TPSA 87.5	✓ Ro5	✓ Clean	`c1cc(c(nc1)C(=O)O)C(=O)O`
PGH RCSB PDB	5F33	Q9X1X7	171.0 Da LogP -1.40 TPSA 116.1	✓ Ro5	✓ Clean	`C(C(=O)NO)OP(=O)(O)O`
PHT RCSB PDB	6G74	Q9X1X7	166.1 Da LogP 1.08 TPSA 74.6	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)O)C(=O)O`
QAS RCSB PDB	6I0P	Q9X1X7	199.2 Da LogP 0.77 TPSA 87.5	✓ Ro5	✓ Clean	`c1cc(nc(c1C(=O)O)C(=O)O)S`
QAT RCSB PDB	6I0R	Q9X1X7	199.2 Da LogP 0.25 TPSA 87.0	✓ Ro5	Alert	`C1C(=S)C=NC(=C1C(=O)O)C(=O)O`
XQB RCSB PDB	6F48	Q9X1X7	203.1 Da LogP -1.26 TPSA 135.8	✓ Ro5	✓ Clean	`[H]/N=C(/[C@H](C[C@@H](C=O)O)C(=O)O)\C(=O)O`
YQA RCSB PDB	6F48	Q9X1X7	185.1 Da LogP -0.75 TPSA 107.2	✓ Ro5	✓ Clean	`C1[C@H](C=NC(=C1C(=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
ZINC1710230 ZINC	1.000	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC2004372 ZINC	0.786	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153 ZINC	0.786	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC135598 ZINC	0.690	227.2 Da LogP 2.01 TPSA 67.3	✓ Ro5	✓ Clean	`O=C(c1ccccc1)c1cccnc1C(=O)O`
ZINC343335 ZINC	0.690	227.2 Da LogP 2.01 TPSA 67.3	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1C(=O)c1ccccc1`
ZINC1296728 ZINC	0.654	244.2 Da LogP 1.54 TPSA 100.4	✓ Ro5	✓ Clean	`O=C(O)c1ncccc1-c1cccnc1C(=O)O`
ZINC47217 ZINC	0.654	244.2 Da LogP 1.54 TPSA 100.4	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1-c1ncccc1C(=O)O`
ZINC151254 ZINC	0.607	202.0 Da LogP 1.54 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1Br`
ZINC2456171 ZINC	0.607	202.0 Da LogP 1.54 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1ncccc1Br`
ZINC39243629 ZINC	0.607	249.0 Da LogP 1.38 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1I`
ZINC5944065 ZINC	0.607	249.0 Da LogP 1.38 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1ncccc1I`
ZINC20272728 ZINC	0.606	209.2 Da LogP 1.34 TPSA 76.5	✓ Ro5	✓ Clean	`CC(C)OC(=O)c1ncccc1C(=O)O`
ZINC59916715 ZINC	0.606	223.2 Da LogP 1.74 TPSA 76.5	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)c1cccnc1C(=O)O`
ZINC72233329 ZINC	0.606	209.2 Da LogP 1.34 TPSA 76.5	✓ Ro5	✓ Clean	`CC(C)OC(=O)c1cccnc1C(=O)O`
ZINC2158679 ZINC	0.588	243.2 Da LogP 1.43 TPSA 92.2	✓ Ro5	✓ Clean	`O=C(Nc1ccccn1)c1cccnc1C(=O)O`
ZINC1857793323 ZINC	0.586	320.3 Da LogP 3.21 TPSA 100.4	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1-c1ccc(-c2ncccc2C(=O)O)cc1`
ZINC142147 ZINC	0.583	219.2 Da LogP 1.62 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1C(=O)N1CCCC1`
ZINC2182270 ZINC	0.583	224.2 Da LogP 0.16 TPSA 88.5	✓ Ro5	✓ Clean	`COCCNC(=O)c1cccnc1C(=O)O`
ZINC2575594 ZINC	0.583	270.3 Da LogP 1.75 TPSA 79.3	✓ Ro5	✓ Clean	`O=C(NCCc1ccccc1)c1cccnc1C(=O)O`
ZINC394746 ZINC	0.583	242.2 Da LogP 2.32 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1C(=O)c1ccc(O)cc1`
ZINC1732721 ZINC	0.571	222.2 Da LogP 1.31 TPSA 79.3	✓ Ro5	✓ Clean	`CCCCNC(=O)c1ncccc1C(=O)O`
ZINC40803118 ZINC	0.571	270.3 Da LogP 1.75 TPSA 79.3	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1C(=O)NCCc1ccccc1`
ZINC4649243 ZINC	0.571	286.2 Da LogP 1.73 TPSA 116.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(NC(=O)c2cccnc2C(=O)O)cc1`
ZINC9694250 ZINC	0.571	286.2 Da LogP 1.73 TPSA 116.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(NC(=O)c2ncccc2C(=O)O)cc1`
ZINC1602105 ZINC	0.565	242.2 Da LogP 2.75 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccccc2)cc1C(=O)O`
ZINC41229465 ZINC	0.563	217.2 Da LogP 2.59 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1ncccc1-c1ccccc1F`
ZINC12137488 ZINC	0.560	247.3 Da LogP 2.40 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1C(=O)N1CCCCCC1`
ZINC143407 ZINC	0.560	221.3 Da LogP 1.91 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)(C)NC(=O)c1ccccc1C(=O)O`
ZINC167015 ZINC	0.560	205.3 Da LogP 2.38 TPSA 40.5	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1N1CCCCC1`
ZINC1707321 ZINC	0.560	223.2 Da LogP 0.20 TPSA 103.7	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)c1ccccc1C(=O)O`
ZINC185924 ZINC	0.560	249.3 Da LogP 2.64 TPSA 57.6	✓ Ro5	✓ Clean	`CC(C)N(C(=O)c1ccccc1C(=O)O)C(C)C`
ZINC19367005 ZINC	0.560	224.4 Da LogP 2.83 TPSA 24.1	✓ Ro5	✓ Clean	`C1CCC(NCCNC2CCCCC2)CC1`
ZINC2584518 ZINC	0.560	222.2 Da LogP 2.34 TPSA 63.6	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)c1ccccc1C(=O)O`
ZINC267002 ZINC	0.560	215.3 Da LogP 2.79 TPSA 42.2	✓ Ro5	Alert	`Cc1ccc(C)n1-c1ccccc1C(=O)O`
ZINC28115 ZINC	0.560	233.3 Da LogP 2.01 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1C(=O)N1CCCCC1`
ZINC34519769 ZINC	0.560	241.2 Da LogP 2.20 TPSA 80.4	✓ Ro5	✓ Clean	`Nc1ccc(C(=O)c2ccccc2C(=O)O)cc1`
ZINC3847474 ZINC	0.560	240.3 Da LogP 2.92 TPSA 54.4	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)c2ccccc2C(=O)O)cc1`
ZINC4729531 ZINC	0.560	217.2 Da LogP 0.81 TPSA 74.7	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1N1C(=O)C=CC1=O`
ZINC56439 ZINC	0.560	244.2 Da LogP 2.75 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1C(=O)c1ccc(F)cc1`
ZINC5760826 ZINC	0.560	208.2 Da LogP 1.95 TPSA 63.6	✓ Ro5	✓ Clean	`CC(C)OC(=O)c1ccccc1C(=O)O`
ZINC60221109 ZINC	0.560	224.2 Da LogP 0.63 TPSA 100.9	✓ Ro5	✓ Clean	`O=C(O)COC(=O)c1ccccc1C(=O)O`
ZINC26468763 ZINC	0.559	243.3 Da LogP -1.35 TPSA 100.5	✓ Ro5	✓ Clean	`O=S(=O)(O)CCN[C@@H]1CCS(=O)(=O)C1`
ZINC26468770 ZINC	0.559	243.3 Da LogP -1.35 TPSA 100.5	✓ Ro5	✓ Clean	`O=S(=O)(O)CCN[C@H]1CCS(=O)(=O)C1`
ZINC1563686 ZINC	0.556	257.2 Da LogP 2.02 TPSA 76.5	✓ Ro5	✓ Clean	`COc1ccc(C(=O)c2cccnc2C(=O)O)cc1`
ZINC5188799 ZINC	0.556	280.5 Da LogP 4.39 TPSA 24.1	✓ Ro5	✓ Clean	`C(CCCNC1CCCCC1)CCNC1CCCCC1`
ZINC6701074 ZINC	0.556	243.2 Da LogP 1.43 TPSA 92.2	✓ Ro5	✓ Clean	`O=C(Nc1cccnc1)c1cccnc1C(=O)O`
ZINC82485552 ZINC	0.556	220.2 Da LogP 0.92 TPSA 79.3	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1C(=O)NCC1CC1`
ZINC95938319 ZINC	0.550	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`
ZINC6471224 ZINC	0.548	203.2 Da LogP 0.03 TPSA 104.6	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1S(=O)(=O)O`
ZINC65347090 ZINC	0.548	215.2 Da LogP 2.15 TPSA 70.4	✓ Ro5	✓ Clean	`O=C(O)c1ncccc1-c1ccccc1O`

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.

Cross-references

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

Sequence

UniProt A0A0H3GU73

Pathways

KEGG R04292 BioCyc QUINOLINATE-SYNTHA-RXN