Protein profile

KP13_00869

Inosine-5'-monophosphate dehydrogenase

Genome: KpKP13

Gene: guaB AHE43232.1 Structure source: AlphaFold + ColabFold UniProt W8UE92

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Amino acids 488

Annotations 9

Features 33

PDB binders 14

Druggability 0.501

Overview

Basic information about this protein and its source genome.

Accession: KP13_00869
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: guaB AHE43232.1
Status: annotated
Amino acids: 488
Structure source: AlphaFold + ColabFold

1.1.1.205

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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 50.413
Human E-value: 6.61e-27
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 98.156
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 91.49

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.501

Structure W8UE92

Pocket Pocket 33

P2Rank 0.952

Structure W8UE92

Pocket Pocket 1

ColabFold model

FPocket 0.498 · Pocket 36

P2Rank 0.956 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 2269 / 4744 genomes with a hit

Normalized 0.478

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

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 Features

Domain/signature hits 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; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_W8UE92	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00869	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
33				0.501
31				0.31

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	29.58	0.932
2	6.47	0.327
3	4.76	0.21
4	3.28	0.114
5	3.12	0.105

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
36				0.498

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	30.07	0.933
2	6.67	0.339
3	4.39	0.184
4	3.51	0.129
5	2.36	0.062

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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	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	4MZ8	Q0P9J4	46.1 Da LogP 0.26 TPSA 9.2	✓ Ro5	✓ Clean	`COC`
8L1	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	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	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	4MZ8	Q0P9J4	378.4 Da LogP 4.89 TPSA 59.8	✓ Ro5	✓ Clean	`c1ccc2cc(ccc2c1)NC(=O)Cn3c4ccccc4nc3c5ccccn5`
IMP	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	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	4MY9	A0A6L8P2U9	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MOA	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	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	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	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	A0A6L8P2U9	8.82	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	A0A6L8P2U9	8.70	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	A0A6L8P2U9	8.64	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	A0A6L8P2U9	8.30	427.3 Da LogP 5.64 TPSA 80.1	1 viol.	✓ Clean	`C[C@@H](C(=O)Nc1ccc2c(c1)nc(o2)c3ccncc3)Nc4cccc…`
CHEMBL2178652	A0A6L8P2U9	8.10	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	A0A6L8P2U9	8.00	428.3 Da LogP 5.60 TPSA 77.2	1 viol.	✓ Clean	`C[C@H](Oc1cccc(Cl)c1Cl)C(=O)Nc1ccc2nc(-c3ccncc3…`
CHEMBL2348796	A0A6L8P2U9	8.00	428.3 Da LogP 5.60 TPSA 77.2	1 viol.	✓ Clean	`C[C@H](Oc1cccc(Cl)c1Cl)C(=O)Nc1ccc2oc(-c3ccncc3…`
CHEMBL3329564	A0A6L8P2U9	7.85	438.8 Da LogP 4.86 TPSA 120.4	✓ Ro5	✓ Clean	`CC(Oc1cccc([N+](=O)[O-])c1Cl)C(=O)Nc1ccc2oc(-c3…`
Q21	A0A6L8P2U9	7.77	409.4 Da LogP 5.45 TPSA 77.3	1 viol.	✓ Clean	`C[C@@H](C(=O)Nc1ccc2c(c1)nc(o2)c3ccncc3)Oc4cccc…`
2YA	A0A6L8P2U9	7.42	366.8 Da LogP 3.85 TPSA 66.9	✓ Ro5	Alert	`C[C@H](c1cn(nn1)c2ccc(cc2)Cl)Oc3cc[n+](c4c3cccc…`
CHEMBL3329561	A0A6L8P2U9	7.02	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	A0A6L8P2U9	7.00	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	A0A6L8P2U9	6.92	353.8 Da LogP 5.54 TPSA 38.3	1 viol.	✓ Clean	`CC(C)C(Oc1cccc2ccccc12)C(=O)Nc1ccc(Cl)cc1`
CHEMBL564117	A0A6L8P2U9	6.80	351.8 Da LogP 5.29 TPSA 38.3	1 viol.	✓ Clean	`O=C(Nc1ccc(Cl)cc1)C(Oc1cccc2ccccc12)C1CC1`
CHEMBL2348631	A0A6L8P2U9	6.52	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	A0A6L8P2U9	6.05	343.4 Da LogP 4.63 TPSA 68.0	✓ Ro5	✓ Clean	`C[C@H](C(=O)Nc1ccc2oc(-c3ccncc3)nc2c1)c1ccccc1`
CHEMBL4459529	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	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	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	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	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	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	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	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	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	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	1.000	366.8 Da LogP 3.85 TPSA 66.9	✓ Ro5	Alert	`C[C@@H](Oc1cc[n+]([O-])c2ccccc12)c1cn(-c2ccc(Cl…`
ZINC4353761	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	0.780	328.4 Da LogP 3.74 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1ccccc1`
ZINC276377022	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	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	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	0.759	342.4 Da LogP 4.05 TPSA 59.8	✓ Ro5	✓ Clean	`Cc1cccc(NC(=O)Cn2c(-c3ccccn3)nc3ccccc32)c1`
ZINC174595	0.755	281.3 Da LogP 3.48 TPSA 68.0	✓ Ro5	✓ Clean	`CC(C)C(=O)Nc1ccc2oc(-c3ccncc3)nc2c1`
ZINC73310355	0.755	362.8 Da LogP 4.39 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1ccc(Cl)cc1`
ZINC225456440	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	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	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	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	0.745	362.8 Da LogP 4.39 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1cccc(Cl)c1`
ZINC2112750699	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	0.740	329.4 Da LogP 3.13 TPSA 72.7	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1ccccn1`
ZINC1857532075	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	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	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	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	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	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.