KpATCC43816 Protein target profile

6,7-dimethyl-8-ribityllumazine synthase

Accession: VK055_2187

Gene: ribH AIK80792.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GJ29

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Length 156

Pocket druggability (P2Rank · AlphaFold DB model) 0.204

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 4 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 97.6% 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: 24.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 100.0 Higher values support similarity to known essential genes.
DEG E-value: 9.180000000000001e-110 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 98.08 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) 0.204

Structure A0A0H3GJ29

Pocket Pocket 1

Druggability (FPocket) 0.681

Structure A0A0H3GJ29

Pocket Pocket 1

ColabFold model

P2Rank 0.291 · Pocket 1

FPocket 0.336 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 1145 / 4744 genomes with a hit

Prevalence 24.1%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing & consuming chokepoint reaction in Riboflavin metabolism, no isoenzyme backup detected, more central than 97.6% of genes in this genome, no human homolog detected.

Relative network centrality 97.6% more central than 97.6% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MNIIEANVATPDARVAITIARFNNFINDSLLEGAIDALKRIGQVKDENITVVWVPGAYELPLAAGALAKTGKYDAVIALGTVIRGGTAHFEYVAGGASNGLAHVAQDSEIPVAFGVLTTESIEQAIERAGTKAGNKGAEAALTALEMINVLKAIKA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.5.1.78

Gene Ontology (GO)

GO:0009231 The chemical reactions and pathways resulting in the formation of riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
GO:0009349 An flavoprotein that catalyzes the reaction the breakdown of dimethyl(ribityl)lumazine to form riboflavin and ribitylamino-amino-dihydroxypyrimidine.
GO:0000906 Catalysis of the reaction: 3,4-dihydroxy-2-butanone-4-phosphate + 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione = 6,7-dimethyl-8-ribityllumazine + phosphate.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

15 records

Show feature table

Start	End	DB	Term	Name
15	148	CDD	cd09209	Lumazine_synthase-I
15	148	InterPro	IPR034964	Lumazine synthase
1	156	Gene3D	G3DSA:3.40.50.960	Lumazine/riboflavin synthase
1	156	InterPro	IPR036467	Lumazine/riboflavin synthase superfamily
1	156	FunFam	G3DSA:3.40.50.960:FF:000001	6,7-dimethyl-8-ribityllumazine synthase
13	151	Pfam	PF00885	6,7-dimethyl-8-ribityllumazine synthase
13	151	InterPro	IPR002180	Lumazine/riboflavin synthase
8	154	Hamap	MF_00178	6,7-dimethyl-8-ribityllumazine synthase [ribH].
8	154	InterPro	IPR034964	Lumazine synthase
4	154	SUPERFAMILY	SSF52121	Lumazine synthase
4	154	InterPro	IPR036467	Lumazine/riboflavin synthase superfamily
14	150	NCBIfam	TIGR00114	6,7-dimethyl-8-ribityllumazine synthase
14	150	InterPro	IPR034964	Lumazine synthase
9	155	PANTHER	PTHR21058	6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE DMRL SYNTHASE LUMAZINE SYNTHASE
9	155	InterPro	IPR034964	Lumazine synthase

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

0.204

Likely same site as FPocket 1 3.2 Å 11 shared residues 100% of smaller site

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.681 Unusual size

Likely same site as P2Rank 1 3.2 Å 11 shared residues 100% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:89-89 Proton donor

UniProt: Binding site:114-114

UniProt: Binding site:128-128

UniProt: Binding site:22-22

UniProt: Binding site:57-59

UniProt: Binding site:81-83

UniProt: Binding site:86-87

Residue sets

UniProt: Active site:89-89 Proton donor

UniProt: Binding site:114-114

UniProt: Binding site:128-128

UniProt: Binding site:22-22

UniProt: Binding site:57-59

UniProt: Binding site:81-83

UniProt: Binding site:86-87

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_A0A0H3GJ29	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2187	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.

58 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5YL PDB via homolog 411.3 Da · LogP -2.56 · TPSA 216.2 Open detail RCSB PDB

CRM PDB via homolog Detail RCSB PDB

DLZ PDB via homolog Detail RCSB PDB

INI PDB via homolog Detail RCSB PDB

LMZ 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
5YL RCSB PDB	1NQW	O66529	411.3 Da LogP -2.56 TPSA 216.2	1 viol.	✓ Clean	`C(CCC1=C(NC(=O)NC1=O)NC[C@@H]([C@@H]([C@@H](CO)…`
CRM RCSB PDB	1KYX	Q9UUB1	386.3 Da LogP -4.13 TPSA 218.8	1 viol.	✓ Clean	`C(CC(=O)O)C1=NC2=C(NC(=O)NC2=O)N(C1=O)C[C@@H]([…`
DLZ RCSB PDB	4KQ6	Q6FXA8	326.3 Da LogP -2.88 TPSA 161.6	✓ Ro5	✓ Clean	`CC1=C(N(C2=NC(=O)NC(=O)C2=N1)C[C@@H]([C@@H]([C@…`
INI RCSB PDB	1RVV	P11998	306.2 Da LogP -3.54 TPSA 201.8	1 viol.	✓ Clean	`C([C@@H]([C@@H]([C@@H](CO)O)O)O)NC1=C(C(=O)NC(=…`
LMZ RCSB PDB	1NQV	O66529	290.2 Da LogP -3.05 TPSA 188.1	1 viol.	✓ Clean	`C([C@@H]([C@@H]([C@@H](CO)O)O)O)NC1=C(C(=O)NC(=…`
RBF RCSB PDB	1KYV	Q9UUB1	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@…`
RDL RCSB PDB	1NQU	O66529	330.3 Da LogP -4.86 TPSA 201.5	1 viol.	✓ Clean	`C([C@@H]([C@@H]([C@@H](CO)O)O)O)N1C2=C(C(=O)NC(…`
RLP RCSB PDB	1NQX	O66529	386.3 Da LogP -3.77 TPSA 219.1	2 viol.	✓ Clean	`C(CC(=O)O)C1=C(N(C2=NC(=O)NC(=O)C2=N1)C[C@@H]([…`

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
ZINC1703511 ZINC	0.679	375.4 Da LogP -1.12 TPSA 148.7	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC4878448 ZINC	0.679	375.4 Da LogP -1.12 TPSA 148.7	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC4878449 ZINC	0.679	375.4 Da LogP -1.12 TPSA 148.7	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC4878453 ZINC	0.679	375.4 Da LogP -1.12 TPSA 148.7	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC4353346 ZINC	0.673	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1ccc2c(nc3c(=O)[nH]c(=O)nc-3n2C[C@H](O)[C@H](…`
ZINC3869414 ZINC	0.667	276.2 Da LogP -3.87 TPSA 184.7	1 viol.	✓ Clean	`Nc1c(NC[C@H](O)[C@H](O)[C@H](O)CO)[nH]c(=O)[nH]…`
ZINC4096380 ZINC	0.647	326.3 Da LogP -2.88 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1nc2c(=O)[nH]c(=O)nc-2n(C[C@H](O)[C@H](O)[C@H…`
ZINC1731984 ZINC	0.643	392.4 Da LogP -2.49 TPSA 175.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)[n+]([O-])c1c(=O)[nH]c(=O)nc-1n2C[…`
ZINC5011745 ZINC	0.643	392.4 Da LogP -2.49 TPSA 175.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)[n+]([O-])c1c(=O)[nH]c(=O)nc-1n2C[…`
ZINC5011746 ZINC	0.643	392.4 Da LogP -2.49 TPSA 175.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)[n+]([O-])c1c(=O)[nH]c(=O)nc-1n2C[…`
ZINC5011747 ZINC	0.643	392.4 Da LogP -2.49 TPSA 175.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)[n+]([O-])c1c(=O)[nH]c(=O)nc-1n2C[…`
ZINC1602641 ZINC	0.615	284.3 Da LogP 0.40 TPSA 97.7	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(CC=O)c2cc1C`
ZINC43214974 ZINC	0.607	373.4 Da LogP -0.51 TPSA 124.3	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(CCN(CCO)CCO)c2cc1C`
ZINC1712550 ZINC	0.596	342.4 Da LogP 1.15 TPSA 106.9	✓ Ro5	✓ Clean	`CCC(=O)OCCn1c2nc(=O)[nH]c(=O)c-2nc2cc(C)c(C)cc21`
ZINC1666568 ZINC	0.589	328.3 Da LogP 0.76 TPSA 106.9	✓ Ro5	✓ Clean	`CC(=O)OCCn1c2nc(=O)[nH]c(=O)c-2nc2cc(C)c(C)cc21`
ZINC4878473 ZINC	0.561	347.3 Da LogP -1.74 TPSA 148.7	✓ Ro5	✓ Clean	`O=c1nc2n(C[C@H](O)[C@H](O)[C@H](O)CO)c3ccccc3cc…`
ZINC4878477 ZINC	0.561	347.3 Da LogP -1.74 TPSA 148.7	✓ Ro5	✓ Clean	`O=c1nc2n(C[C@@H](O)[C@H](O)[C@H](O)CO)c3ccccc3c…`
ZINC4878479 ZINC	0.561	347.3 Da LogP -1.74 TPSA 148.7	✓ Ro5	✓ Clean	`O=c1nc2n(C[C@H](O)[C@@H](O)[C@H](O)CO)c3ccccc3c…`
ZINC4878481 ZINC	0.561	347.3 Da LogP -1.74 TPSA 148.7	✓ Ro5	✓ Clean	`O=c1nc2n(C[C@@H](O)[C@@H](O)[C@H](O)CO)c3ccccc3…`
ZINC391159 ZINC	0.560	256.3 Da LogP 0.74 TPSA 80.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C)c2cc1C`
ZINC100069844 ZINC	0.542	363.3 Da LogP -2.03 TPSA 168.9	1 viol.	✓ Clean	`O=c1nc2n(C[C@H](O)[C@H](O)[C@H](O)CO)c3cc(O)ccc…`
ZINC1666570 ZINC	0.541	386.4 Da LogP 0.61 TPSA 144.2	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(CCOC(=O)CCC(=O)O)c…`
ZINC43214973 ZINC	0.541	393.8 Da LogP -0.17 TPSA 124.3	✓ Ro5	✓ Clean	`Cc1cc2c(cc1Cl)nc1c(=O)[nH]c(=O)nc-1n2CCN(CCO)CCO`
ZINC1870669 ZINC	0.534	353.4 Da LogP -0.09 TPSA 137.1	✓ Ro5	✓ Clean	`COC(=O)Nc1nc2cc(C)c(C)cc2n1C[C@@H](O)[C@@H](O)[…`
ZINC4830947 ZINC	0.534	353.4 Da LogP -0.09 TPSA 137.1	✓ Ro5	✓ Clean	`COC(=O)Nc1nc2cc(C)c(C)cc2n1C[C@H](O)[C@H](O)[C@…`
ZINC4830948 ZINC	0.534	353.4 Da LogP -0.09 TPSA 137.1	✓ Ro5	✓ Clean	`COC(=O)Nc1nc2cc(C)c(C)cc2n1C[C@@H](O)[C@H](O)[C…`
ZINC4830949 ZINC	0.534	353.4 Da LogP -0.09 TPSA 137.1	✓ Ro5	✓ Clean	`COC(=O)Nc1nc2cc(C)c(C)cc2n1C[C@H](O)[C@@H](O)[C…`
ZINC11565587 ZINC	0.533	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC1532585 ZINC	0.533	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC1769096 ZINC	0.533	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC2036848 ZINC	0.533	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC3650334 ZINC	0.533	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC3831422 ZINC	0.533	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC3831423 ZINC	0.533	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC3831424 ZINC	0.533	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC4430517 ZINC	0.525	404.4 Da LogP -1.22 TPSA 161.6	✓ Ro5	✓ Clean	`CCc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)…`
ZINC4353442 ZINC	0.524	357.4 Da LogP 0.02 TPSA 131.1	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C/C=N/NC(N)=S)c2cc…`
ZINC8580591 ZINC	0.524	357.4 Da LogP 0.02 TPSA 131.1	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C/C=N\NC(N)=S)c2cc…`
ZINC1722914 ZINC	0.516	393.8 Da LogP -0.17 TPSA 124.3	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(CCN(CCO)CCO)c2cc1Cl`
ZINC5012547 ZINC	0.516	455.4 Da LogP -1.00 TPSA 195.2	1 viol.	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC1562485 ZINC	0.508	374.4 Da LogP -0.51 TPSA 135.8	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)cc-3n(C[C@@H](O)[C@H](O)…`
ZINC5372514 ZINC	0.508	374.4 Da LogP -0.51 TPSA 135.8	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)cc-3n(C[C@H](O)[C@H](O)[…`
ZINC5372517 ZINC	0.508	374.4 Da LogP -0.51 TPSA 135.8	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)cc-3n(C[C@H](O)[C@@H](O)…`
ZINC5372519 ZINC	0.508	374.4 Da LogP -0.51 TPSA 135.8	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)cc-3n(C[C@@H](O)[C@@H](O…`
ZINC4353342 ZINC	0.508	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC4353343 ZINC	0.508	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC4353345 ZINC	0.508	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC4430765 ZINC	0.508	447.2 Da LogP -1.67 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO)c3…`
ZINC4430766 ZINC	0.508	447.2 Da LogP -1.67 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO)c…`
ZINC4430768 ZINC	0.508	447.2 Da LogP -1.67 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO)…`

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 A0A0H3GJ29

Pathways

KEGG R04457 BioCyc LUMAZINESYN-RXN