KpKP13 Protein target profile

Inosine-5'-monophosphate dehydrogenase

Accession: KP13_00869

Gene: guaB AHE43232.1 3D evidence: AlphaFold DB model + ColabFold model UniProt W8UE92

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Length 488

Pocket druggability (P2Rank · AlphaFold DB model) 0.952

Direct ligand evidence 0 83 total records

Functional annotation 1 EC 8 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 0.50. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.95. 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 (%): 50.413 Lower values reduce human off-target concern.
Human E-value: 6.61e-27
Gut microbiome similarity: 47.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 98.156 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 91.49 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) 0.952

Structure W8UE92

Pocket Pocket 1

Druggability (FPocket) 0.501

Structure W8UE92

Pocket Pocket 33

ColabFold model

P2Rank 0.956 · Pocket 1

FPocket 0.498 · Pocket 36

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 2269 / 4744 genomes with a hit

Prevalence 47.8%

Sequence

Primary amino-acid sequence viewer.

MLRIAKEALTFDDVLLVPAHSTVLPNTADLSTQLTKTIRLNIPMLSAAMDTVTEARLAIALAQEGGIGFIHKNMSIERQAEEVRRVKKHESGVVTDPQTVLPTTTLREVKELTERNGFAGYPVVTEENELVGIITGRDVRFVTDLNQPVSVYMTPKERLVTVREGESREVVFAKMHEKRVEKALVVDESFHLRGMITVKDFQKAERKPNACKDEQGRLRVGAAVGAGAGNEERVDALVAAGVDVLLIDSSHGHSEGVLQRIRETRAKYPDLQIIGGNVATGAGARALAEAGCSAVKVGIGPGSICTTRIVTGVGVPQITAVSDAVEALEGTGIPVIADGGIRFSGDIAKAIAAGAAAVMVGSMLAGTEESPGEIELYQGRSYKSYRGMGSLGAMSKGSSDRYFQSDNAADKLVPEGIEGRVAYKGRLKEIIHQQMGGLRSCMGLTGCGTIDLLRTKAEFVRISGAGIQESHVHDVTITKESPNYRLGS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.1.1.205

Gene Ontology (GO)

GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0003938 Catalysis of the reaction: inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+.
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:0006164 The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
GO:0046872 Binding to a metal ion.
GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
GO:0006177 The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate.
GO:0006183 The chemical reactions and pathways resulting in the formation of GTP, guanosine triphosphate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
8	486	Hamap	MF_01964	Inosine-5'-monophosphate dehydrogenase [guaB].
8	486	InterPro	IPR005990	Inosine-5'-monophosphate dehydrogenase
6	481	PANTHER	PTHR11911	INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED
6	481	InterPro	IPR005990	Inosine-5'-monophosphate dehydrogenase
94	203	SUPERFAMILY	SSF54631	CBS-domain pair
94	203	InterPro	IPR046342	CBS domain superfamily
7	473	SMART	SM01240	IMPDH_2
8	454	NCBIfam	TIGR01302	IMP dehydrogenase
8	454	InterPro	IPR005990	Inosine-5'-monophosphate dehydrogenase
158	206	SMART	SM00116	cbs_1
158	206	InterPro	IPR000644	CBS domain
96	144	SMART	SM00116	cbs_1
96	144	InterPro	IPR000644	CBS domain
8	462	CDD	cd00381	IMPDH
8	462	InterPro	IPR001093	IMP dehydrogenase/GMP reductase
295	307	ProSitePatterns	PS00487	IMP dehydrogenase / GMP reductase signature.
295	307	InterPro	IPR015875	IMP dehydrogenase / GMP reductase, conserved site
153	202	Pfam	PF00571	CBS domain
153	202	InterPro	IPR000644	CBS domain
95	140	Pfam	PF00571	CBS domain
95	140	InterPro	IPR000644	CBS domain
1	487	PIRSF	PIRSF000130	IMPDH
1	487	InterPro	IPR005990	Inosine-5'-monophosphate dehydrogenase
1	486	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	486	InterPro	IPR013785	Aldolase-type TIM barrel
93	149	ProSiteProfiles	PS51371	CBS domain profile.
93	149	InterPro	IPR000644	CBS domain
1	486	FunFam	G3DSA:3.20.20.70:FF:000003	GMP reductase
153	214	ProSiteProfiles	PS51371	CBS domain profile.
153	214	InterPro	IPR000644	CBS domain
8	473	Pfam	PF00478	IMP dehydrogenase / GMP reductase domain
8	473	InterPro	IPR001093	IMP dehydrogenase/GMP reductase
1	477	SUPERFAMILY	SSF51412	Inosine monophosphate dehydrogenase (IMPDH)

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

0.952

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Surrounding area

Pocket 2 P2Rank #2

0.47

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Surrounding area

Pocket 3 P2Rank #3

0.245

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Surrounding area

Pocket 4 P2Rank #4

0.208

Likely same site as FPocket 31 5.0 Å 13 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.15

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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 #33

0.501

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Surrounding area

Pocket 2 FPocket #31

0.31 Unusual size

Likely same site as P2Rank 4 5.0 Å 13 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.956

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Surrounding area

Pocket 2 P2Rank #2

0.485

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Surrounding area

Pocket 3 P2Rank #3

0.193

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Surrounding area

Pocket 4 P2Rank #4

0.172

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Surrounding area

Pocket 5 P2Rank #5

0.118

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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_W8UE92	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00869	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.

83 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 33 records from similar proteins

Structural ligands 14 0 loaded crystals

Measured bioactivity 19 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2EY PDB via homolog 366.8 Da · LogP 3.90 · TPSA 72.8 Open detail RCSB PDB

2F1 PDB via homolog Detail RCSB PDB

2F2 PDB via homolog Detail RCSB PDB

8L1 PDB via homolog Detail RCSB PDB

8L4 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
2EY RCSB PDB	4MYA	A0A6L8P2U9	366.8 Da LogP 3.90 TPSA 72.8	✓ Ro5	✓ Clean	`C[C@H](c1cn(nn1)c2ccc(cc2)Cl)OC3=CC(=O)Nc4c3ccc…`
2F1 RCSB PDB	4MZ1	Q0P9J4	373.3 Da LogP 5.54 TPSA 41.1	1 viol.	✓ Clean	`CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(cc2)Br`
2F2 RCSB PDB	4MZ8	Q0P9J4	46.1 Da LogP 0.26 TPSA 9.2	✓ Ro5	✓ Clean	`COC`
8L1 RCSB PDB	5UUV	A0A6L8P2U9	496.9 Da LogP 6.74 TPSA 86.6	1 viol.	✓ Clean	`C/C(=N\O)/c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)c3…`
8L4 RCSB PDB	5UUZ	A0A6L8P2U9	346.8 Da LogP 3.70 TPSA 97.2	✓ Ro5	✓ Clean	`[H]/N=C(/c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(cc2)Cl)\…`
8LA RCSB PDB	5URS	A0A6L8P2U9	477.0 Da LogP 3.25 TPSA 120.3	✓ Ro5	✓ Clean	`CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)O[C@@H…`
C91 RCSB PDB	4MZ8	Q0P9J4	378.4 Da LogP 4.89 TPSA 59.8	✓ Ro5	✓ Clean	`c1ccc2cc(ccc2c1)NC(=O)Cn3c4ccccc4nc3c5ccccn5`
IMP RCSB PDB	1ZFJ	P0C0H6	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…`
JQS RCSB PDB	6MGU	A0A6L8P2U9	366.2 Da LogP -2.07 TPSA 209.9	1 viol.	✓ Clean	`c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O…`
MLI RCSB PDB	4MY9	A0A6L8P2U9	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MOA RCSB PDB	4FO4	Q9KTW3	320.3 Da LogP 2.73 TPSA 93.1	✓ Ro5	✓ Clean	`Cc1c2c(c(c(c1OC)C\C=C(/C)\CCC(=O)O)O)C(=O)OC2`
NAJ RCSB PDB	4QNE	Q9KTW3	663.4 Da LogP -4.86 TPSA 325.2	3 viol.	✓ Clean	`c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)COP(…`
TAR RCSB PDB	3TSD	A0A6L8P2U9	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@@H](C(=O)O)O)(C(=O)O)O`
XMP RCSB PDB	4X3Z	Q9KTW3	365.2 Da LogP -3.44 TPSA 201.2	1 viol.	✓ Clean	`c1[nH+]c2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=…`

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
2F0 ChEMBL	A0A6L8P2U9	8.82 ~1.5 nM	388.9 Da LogP 3.69 TPSA 116.8	✓ Ro5	✓ Clean	`C/C(=N\O)/c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)C(…`
CHEMBL2178644 ChEMBL	A0A6L8P2U9	8.70 ~2.0 nM	413.8 Da LogP 5.61 TPSA 73.7	1 viol.	✓ Clean	`C/C(=N\O)c1cccc(C(C)(C)NC(=O)Nc2ccc(Cl)c(C(F)(F…`
P68 ChEMBL	A0A6L8P2U9	8.64 ~2.3 nM	390.3 Da LogP 4.70 TPSA 73.7	✓ Ro5	✓ Clean	`C/C(=N\O)/c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(cc2)Br`
Q67 ChEMBL	A0A6L8P2U9	8.30 ~5.0 nM	427.3 Da LogP 5.64 TPSA 80.1	1 viol.	✓ Clean	`C[C@@H](C(=O)Nc1ccc2c(c1)nc(o2)c3ccncc3)Nc4cccc…`
CHEMBL2178652 ChEMBL	A0A6L8P2U9	8.10 ~7.9 nM	396.8 Da LogP 6.45 TPSA 41.1	1 viol.	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(Cl)c(C(F)(F)F)…`
CHEMBL2348627 ChEMBL	A0A6L8P2U9	8.00 ~10.0 nM	428.3 Da LogP 5.60 TPSA 77.2	1 viol.	✓ Clean	`C[C@H](Oc1cccc(Cl)c1Cl)C(=O)Nc1ccc2nc(-c3ccncc3…`
CHEMBL2348796 ChEMBL	A0A6L8P2U9	8.00 ~10.0 nM	428.3 Da LogP 5.60 TPSA 77.2	1 viol.	✓ Clean	`C[C@H](Oc1cccc(Cl)c1Cl)C(=O)Nc1ccc2oc(-c3ccncc3…`
CHEMBL3329564 ChEMBL	A0A6L8P2U9	7.85 ~14.1 nM	438.8 Da LogP 4.86 TPSA 120.4	✓ Ro5	✓ Clean	`CC(Oc1cccc([N+](=O)[O-])c1Cl)C(=O)Nc1ccc2oc(-c3…`
Q21 ChEMBL	A0A6L8P2U9	7.77 ~17.0 nM	409.4 Da LogP 5.45 TPSA 77.3	1 viol.	✓ Clean	`C[C@@H](C(=O)Nc1ccc2c(c1)nc(o2)c3ccncc3)Oc4cccc…`
2YA ChEMBL	A0A6L8P2U9	7.42 ~38.0 nM	366.8 Da LogP 3.85 TPSA 66.9	✓ Ro5	Alert	`C[C@H](c1cn(nn1)c2ccc(cc2)Cl)Oc3cc[n+](c4c3cccc…`
CHEMBL3329561 ChEMBL	A0A6L8P2U9	7.02 ~95.5 nM	380.3 Da LogP 5.25 TPSA 73.7	1 viol.	✓ Clean	`C/C(=N\O)c1cccc(C(C)(C)NC(=O)Nc2ccc(Cl)c(Cl)c2)…`
CHEMBL3329563 ChEMBL	A0A6L8P2U9	7.00 ~100.0 nM	472.0 Da LogP 3.98 TPSA 97.3	✓ Ro5	✓ Clean	`C/C(=N\O)c1cccc(C(C)(C)NC(=O)Nc2ccc(Cl)c(C(=O)N…`
CHEMBL557281 ChEMBL	A0A6L8P2U9	6.92 ~120.2 nM	353.8 Da LogP 5.54 TPSA 38.3	1 viol.	✓ Clean	`CC(C)C(Oc1cccc2ccccc12)C(=O)Nc1ccc(Cl)cc1`
CHEMBL564117 ChEMBL	A0A6L8P2U9	6.80 ~158.5 nM	351.8 Da LogP 5.29 TPSA 38.3	1 viol.	✓ Clean	`O=C(Nc1ccc(Cl)cc1)C(Oc1cccc2ccccc12)C1CC1`
CHEMBL2348631 ChEMBL	A0A6L8P2U9	6.52 ~302.0 nM	430.3 Da LogP 5.05 TPSA 80.3	1 viol.	✓ Clean	`C[C@H](Oc1cccc(Cl)c1Cl)C(=O)Nc1cccc(NC(=O)c2ccn…`
CHEMBL2348634 ChEMBL	A0A6L8P2U9	6.05 ~891.3 nM	343.4 Da LogP 4.63 TPSA 68.0	✓ Ro5	✓ Clean	`C[C@H](C(=O)Nc1ccc2oc(-c3ccncc3)nc2c1)c1ccccc1`
CHEMBL4459529 ChEMBL	Q9HXM5	—	327.3 Da LogP 0.19 TPSA 167.9	✓ Ro5	✓ Clean	`N#CC1=C(N)Oc2[nH]c(=O)[nH]c(=O)c2C1c1ccc([N+](=…`
CHEMBL4581243 ChEMBL	Q9HXM5	—	333.3 Da LogP 0.25 TPSA 167.9	✓ Ro5	✓ Clean	`N#CC1=C(N)Oc2[nH]c(=O)[nH]c(=O)c2C1c1ccc([N+](=…`
F2K ChEMBL	Q9HXM5	—	316.7 Da LogP 0.93 TPSA 124.8	✓ Ro5	✓ Clean	`c1cc(ccc1C2C(=C(OC3=C2C(=O)NC(=O)N3)N)C#N)Cl`

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
ZINC14951284 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC1532551 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC16969369 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC1758 ZINC	1.000	320.3 Da LogP 2.73 TPSA 93.1	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1C/C=C(\C)CCC(=O)O)C(=O)OC2`
ZINC1903846686 ZINC	1.000	320.3 Da LogP 2.73 TPSA 93.1	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1CC=C(C)CCC(=O)O)C(=O)OC2`
ZINC2014826 ZINC	1.000	320.3 Da LogP 2.73 TPSA 93.1	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1C/C=C(/C)CCC(=O)O)C(=O)OC2`
ZINC4228242 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@…`
ZINC43020550 ZINC	1.000	366.8 Da LogP 3.85 TPSA 66.9	✓ Ro5	Alert	`C[C@@H](Oc1cc[n+]([O-])c2ccccc12)c1cn(-c2ccc(Cl…`
ZINC4353761 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC8614392 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC28824028 ZINC	0.857	334.4 Da LogP 3.04 TPSA 82.1	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(OC)c1C/C=C(\C)CCC(=O)O)C(=O)OC2`
ZINC106686432 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP…`
ZINC12958393 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)O…`
ZINC35024781 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024785 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024786 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)…`
ZINC4261903 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC80601236 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC95921560 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC1178445 ZINC	0.837	351.5 Da LogP 4.73 TPSA 70.2	✓ Ro5	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(NC(C)=O)cc2)c1`
ZINC136730219 ZINC	0.824	319.4 Da LogP 2.13 TPSA 98.9	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1C/C=C(\C)CCC(N)=O)C(=O)OC2`
ZINC22005885 ZINC	0.824	334.4 Da LogP 2.82 TPSA 82.1	✓ Ro5	✓ Clean	`COC(=O)CC/C(C)=C/Cc1c(O)c2c(c(C)c1OC)COC2=O`
ZINC35466166 ZINC	0.811	388.5 Da LogP 4.46 TPSA 93.1	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1C/C=C(\C)CCC/C(C)=C/CC(=O)O)C…`
ZINC454732 ZINC	0.800	336.4 Da LogP 4.98 TPSA 58.2	✓ Ro5	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(C(C)=O)cc2)c1`
ZINC13759728 ZINC	0.796	306.3 Da LogP 2.43 TPSA 104.1	✓ Ro5	✓ Clean	`C/C(=C\Cc1c(O)c(C)c2c(c1O)C(=O)OC2)CCC(=O)O`
ZINC14611617 ZINC	0.792	348.4 Da LogP 3.21 TPSA 82.1	✓ Ro5	✓ Clean	`CCOC(=O)CC/C(C)=C/Cc1c(O)c2c(c(C)c1OC)COC2=O`
ZINC201768706 ZINC	0.792	333.4 Da LogP 2.39 TPSA 84.9	✓ Ro5	✓ Clean	`CNC(=O)CC/C(C)=C/Cc1c(O)c2c(c(C)c1OC)COC2=O`
ZINC67665220 ZINC	0.792	347.4 Da LogP 2.74 TPSA 76.1	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1C/C=C(\C)CCC(=O)N(C)C)C(=O)OC2`
ZINC77319466 ZINC	0.792	364.3 Da LogP -0.78 TPSA 163.0	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(=S)[nH]cnc32)[…`
ZINC4724858 ZINC	0.783	312.4 Da LogP 4.92 TPSA 41.1	✓ Ro5	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(F)cc2)c1`
ZINC28539620 ZINC	0.780	328.4 Da LogP 3.74 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1ccccc1`
ZINC276377022 ZINC	0.778	349.4 Da LogP 2.33 TPSA 94.1	✓ Ro5	✓ Clean	`CONC(=O)CC/C(C)=C/Cc1c(O)c2c(c(C)c1OC)COC2=O`
ZINC77311507 ZINC	0.768	420.5 Da LogP 3.66 TPSA 119.4	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(OCCCCC(=O)O)c1C/C=C(\C)CCC(=O)O)C…`
ZINC286872 ZINC	0.766	337.4 Da LogP 3.88 TPSA 84.2	✓ Ro5	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(C(N)=O)cc2)c1`
ZINC28539779 ZINC	0.759	342.4 Da LogP 4.05 TPSA 59.8	✓ Ro5	✓ Clean	`Cc1cccc(NC(=O)Cn2c(-c3ccccn3)nc3ccccc32)c1`
ZINC174595 ZINC	0.755	281.3 Da LogP 3.48 TPSA 68.0	✓ Ro5	✓ Clean	`CC(C)C(=O)Nc1ccc2oc(-c3ccncc3)nc2c1`
ZINC73310355 ZINC	0.755	362.8 Da LogP 4.39 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1ccc(Cl)cc1`
ZINC225456440 ZINC	0.750	282.3 Da LogP -1.61 TPSA 122.5	✓ Ro5	✓ Clean	`COC[C@@H]1O[C@H](n2cnc3c(=O)[nH]cnc32)[C@H](O)[…`
ZINC230149202 ZINC	0.750	282.3 Da LogP -1.61 TPSA 122.5	✓ Ro5	✓ Clean	`COC[C@@H]1O[C@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)…`
ZINC266599 ZINC	0.750	324.4 Da LogP 4.79 TPSA 50.4	✓ Ro5	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(OC)cc2)c1`
ZINC96116024 ZINC	0.750	361.4 Da LogP 3.17 TPSA 84.9	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1C/C=C(\C)CCC(=O)NC(C)C)C(=O)O…`
ZINC23144110 ZINC	0.745	362.8 Da LogP 4.39 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1cccc(Cl)c1`
ZINC2112750699 ZINC	0.741	360.5 Da LogP 3.98 TPSA 76.0	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1C/C=C(\C)CC/C=C(\C)CCO)C(=O)O…`
ZINC46084891 ZINC	0.740	329.4 Da LogP 3.13 TPSA 72.7	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1ccccn1`
ZINC1857532075 ZINC	0.737	387.5 Da LogP 3.66 TPSA 76.1	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1CC=C(C)CCC(=O)N1CCCCC1)C(=O)O…`
ZINC270936689 ZINC	0.737	387.5 Da LogP 3.66 TPSA 76.1	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1C/C=C(\C)CCC(=O)N1CCCCC1)C(=O…`
ZINC276527516 ZINC	0.737	363.4 Da LogP 2.72 TPSA 94.1	✓ Ro5	✓ Clean	`CCONC(=O)CC/C(C)=C/Cc1c(O)c2c(c(C)c1OC)COC2=O`
ZINC35466162 ZINC	0.737	362.4 Da LogP 3.76 TPSA 93.1	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1C/C=C(\C)CCC[C@@H](C)C(=O)O)C…`
ZINC62001485 ZINC	0.737	359.4 Da LogP 2.93 TPSA 84.9	✓ Ro5	✓ Clean	`COc1c(C)c2c(c(O)c1C/C=C(\C)CCC(=O)NC1CC1)C(=O)O…`
ZINC62001757 ZINC	0.737	391.4 Da LogP 1.94 TPSA 111.2	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CC/C(C)=C/Cc1c(O)c2c(c(C)c1OC)COC…`

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 W8UE92

Chemistry

ChEMBL 2F0 ChEMBL CHEMBL2178644 ChEMBL P68 ChEMBL Q67 ChEMBL CHEMBL2178652 ChEMBL CHEMBL2348627 ChEMBL CHEMBL2348796 ChEMBL CHEMBL3329564 ChEMBL Q21 ChEMBL 2YA ChEMBL CHEMBL3329561 ChEMBL CHEMBL3329563 ChEMBL CHEMBL557281 ChEMBL CHEMBL564117 ChEMBL CHEMBL2348631 ChEMBL CHEMBL2348634 ChEMBL CHEMBL4459529 ChEMBL CHEMBL4581243 ChEMBL F2K