Protein profile

KP13_01719

ATP-dependent DNA helicase recQ

Genome: KpKP13

Gene: recQ AHE46977.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GKF3

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Amino acids 608

Annotations 19

Features 48

PDB binders 4

Druggability 0.635

Overview

Basic information about this protein and its source genome.

Accession: KP13_01719
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: recQ AHE46977.1
Status: annotated
Amino acids: 608
Structure source: AlphaFold + ColabFold

5.6.2.4

GO:0044237 OBSOLETE. The chemical reactions and pathways by which individual cells transform chemical substances. GO:0004386 Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix. GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. GO:0043138 Unwinding a DNA helix in the direction 5' to 3', driven by ATP hydrolysis. GO:0009432 An error-prone process for repairing damaged microbial DNA. GO:0003676 Binding to a nucleic acid.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 55.102
Human E-value: 7.66e-13
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 63.744
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 89.38

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 0.635

Structure A0A0H3GKF3

Pocket Pocket 10

P2Rank 0.948

Structure A0A0H3GKF3

Pocket Pocket 1

ColabFold model

FPocket 0.843 · Pocket 10

P2Rank 0.862 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 140 / 4744 genomes with a hit

Normalized 0.03

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 18 GO

Enzyme Commission (EC)

5.6.2.4

Gene Ontology (GO)

GO:0044237 OBSOLETE. The chemical reactions and pathways by which individual cells transform chemical substances.
GO:0004386 Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
GO:0043138 Unwinding a DNA helix in the direction 5' to 3', driven by ATP hydrolysis.
GO:0009432 An error-prone process for repairing damaged microbial DNA.
GO:0003676 Binding to a nucleic acid.
GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
GO:0006310 Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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:0043590 The region of a bacterial cell to which the DNA is confined.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0030894 A multi-component enzymatic machine at the replication fork which mediates DNA replication. Includes DNA primase, one or more DNA polymerases, DNA helicases, and other proteins.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0009378 Unwinding a DNA helix of DNA containing four-way junctions, including Holliday junctions, driven by ATP hydrolysis.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0046872 Binding to a metal ion.

Sequence Features

Domain/signature hits from InterPro and related databases.

48 records

Show feature table

Start	End	DB	Term	Name
529	608	ProSiteProfiles	PS50967	HRDC domain profile.
529	608	InterPro	IPR002121	HRDC domain
2	208	Gene3D	G3DSA:3.40.50.300	-
2	208	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
341	522	Gene3D	G3DSA:1.10.10.10	-
341	522	InterPro	IPR036388	Winged helix-like DNA-binding domain superfamily
223	371	ProSiteProfiles	PS51194	Superfamilies 1 and 2 helicase C-terminal domain profile.
223	371	InterPro	IPR001650	Helicase, C-terminal
8	201	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
8	201	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
28	187	Pfam	PF00270	DEAD/DEAH box helicase
28	187	InterPro	IPR011545	DEAD/DEAH box helicase domain
529	608	SMART	SM00341	hrdc7
1	209	FunFam	G3DSA:3.40.50.300:FF:000296	ATP-dependent DNA helicase RecQ
526	606	FunFam	G3DSA:1.10.150.80:FF:000002	ATP-dependent DNA helicase RecQ
530	605	SUPERFAMILY	SSF47819	HRDC-like
530	605	InterPro	IPR010997	HRDC-like superfamily
210	340	FunFam	G3DSA:3.40.50.300:FF:000156	ATP-dependent DNA helicase recQ
13	592	PANTHER	PTHR13710	DNA HELICASE RECQ FAMILY MEMBER
15	464	NCBIfam	TIGR00614	RecQ family ATP-dependent DNA helicase
15	464	InterPro	IPR004589	DNA helicase, ATP-dependent, RecQ type
210	340	CDD	cd18794	SF2_C_RecQ
34	202	ProSiteProfiles	PS51192	Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
34	202	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
523	608	Gene3D	G3DSA:1.10.150.80	HRDC domain
523	608	InterPro	IPR044876	HRDC domain superfamily
223	330	Pfam	PF00271	Helicase conserved C-terminal domain
223	330	InterPro	IPR001650	Helicase, C-terminal
533	599	Pfam	PF00570	HRDC domain
533	599	InterPro	IPR002121	HRDC domain
343	404	Pfam	PF16124	RecQ zinc-binding
343	404	InterPro	IPR032284	ATP-dependent DNA helicase RecQ, zinc-binding domain
406	514	Pfam	PF09382	RQC domain
406	514	InterPro	IPR018982	RQC domain
22	218	SMART	SM00487	ultradead3
22	218	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
411	514	SMART	SM00956	RQC_2
411	514	InterPro	IPR018982	RQC domain
14	209	CDD	cd17920	DEXHc_RecQ
13	601	NCBIfam	TIGR01389	DNA helicase RecQ
13	601	InterPro	IPR006293	DNA helicase, ATP-dependent, RecQ type, bacterial
209	340	Gene3D	G3DSA:3.40.50.300	-
209	340	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
341	522	FunFam	G3DSA:1.10.10.10:FF:000175	ATP-dependent DNA helicase RecQ
250	331	SMART	SM00490	helicmild6
250	331	InterPro	IPR001650	Helicase, C-terminal
208	455	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
208	455	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase

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_A0A0H3GKF3	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01719	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
10				0.635

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	22.06	0.877
2	4.79	0.212
3	2.42	0.065
4	1.23	0.011
5	1.0	0.006

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
10				0.843
3				0.773

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	14.47	0.724
2	2.77	0.084
3	1.62	0.026
4	1.1	0.008

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.

78 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
6SV	5LBA	O94762	226.3 Da LogP 1.80 TPSA 50.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NC(=O)NC[C@H]2CCCO2`
AGS	1OYY	P15043	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ANP	4D25	O01378	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
EU3	2FBY	Q14191	152.0 Da LogP 0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Eu+3]`

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
CHEMBL1399702	P54132	8.96	252.2 Da LogP -1.56 TPSA 113.5	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3cncnc32)[C@H](O)[C@@H]1O`
CHEMBL1608159	P54132	8.96	629.6 Da LogP -15.49 TPSA 290.4	2 viol.	✓ Clean	`Nc1nc(Cl)nc2c1ncn2[C@@H]1O[C@H](COP(=O)([O-])OP…`
5AE	P54132	8.80	244.2 Da LogP -3.17 TPSA 143.7	✓ Ro5	✓ Clean	`C1=NC(=NC(=O)N1[C@H]2[C@@H]([C@@H]([C@H](O2)CO)…`
CHEMBL1590552	P54132	8.55	641.2 Da LogP -15.42 TPSA 290.4	2 viol.	✓ Clean	`CSc1nc(N)c2ncn([C@@H]3O[C@H](COP(=O)([O-])OP(=O…`
MZR	P54132	8.55	259.2 Da LogP -2.70 TPSA 151.1	✓ Ro5	✓ Clean	`c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)CO)O)O)O)…`
CHEMBL316966	P54132	8.46	329.2 Da LogP -0.82 TPSA 154.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H]2COP(=O)(O)O[C@H]2[…`
CHEMBL1395737	P54132	8.30	399.4 Da LogP -0.61 TPSA 160.4	✓ Ro5	Alert	`CNC(=O)[C@H]1O[C@@H](n2cnc3c(NCc4ccc(N)cc4)ncnc…`
CHEMBL1394945	P54132	8.05	361.4 Da LogP 0.04 TPSA 125.6	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3c(N[C@H]4CC5CCC4C5)ncnc32…`
CHEMBL1436882	P54132	8.00	358.4 Da LogP -0.24 TPSA 151.6	✓ Ro5	✓ Clean	`Nc1nc(Nc2ccccc2)nc2c1ncn2[C@@H]1O[C@H](CO)[C@H]…`
CHEMBL1475917	P54132	7.90	419.4 Da LogP 0.64 TPSA 156.7	1 viol.	✓ Clean	`O=[N+]([O-])c1ccc(CSc2ncnc3c2ncn3[C@@H]2O[C@H](…`
CHEMBL1596388	P54132	7.60	781.5 Da LogP -6.62 TPSA 353.4	3 viol.	✓ Clean	`NC(=S)c1ccc[n+]([C@@H]2O[C@@H](COP(=O)([O-])OP(…`
CHEMBL1231330	P54132	7.55	149.1 Da LogP -2.16 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@H](C(=O)O)[C@H](O)C(=O)O`
CHEMBL1457622	P54132	7.45	448.1 Da LogP -9.87 TPSA 223.5	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)([O-])OP(=O)([O-])…`
CHEMBL1471192	P46063	7.25	451.6 Da LogP 1.73 TPSA 104.8	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)NCC(=O)N(CC(=O)NC2CCCCC2)CC2CCC…`
CHEMBL18238	P54132	7.15	371.4 Da LogP 0.36 TPSA 125.6	✓ Ro5	✓ Clean	`Cc1ccccc1CNc1ncnc2c1ncn2C1OC(CO)C(O)C1O`
CHEMBL1560762	P46063	6.85	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NCC1CCCO1`
CHEMBL1442153	P54132	6.50	294.3 Da LogP -2.23 TPSA 148.4	✓ Ro5	✓ Clean	`CNC(=O)[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[…`
CHEMBL1446521	P46063	6.50	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NCC3CCCO3)n2C)cc1`
CHEMBL1554131	P54132	6.45	281.3 Da LogP -1.52 TPSA 125.6	✓ Ro5	✓ Clean	`CNc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
CHEMBL64239	P54132	6.40	205.2 Da LogP 0.72 TPSA 78.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2C1CCCO1`
CHEMBL1448630	P46063	6.05	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NCC2CCCO2)cc1`
CHEMBL1057	P46063	—	332.3 Da LogP 3.67 TPSA 76.0	✓ Ro5	✓ Clean	`O=C1OC2(c3ccc(O)cc3Oc3cc(O)ccc32)c2ccccc21`
CHEMBL119171	Q14191	—	299.3 Da LogP -1.69 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(S)c2ncn(C3OC(CO)C(O)C3O)c2n1`
CHEMBL1715183	Q14191	—	803.9 Da LogP 4.01 TPSA 236.7	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCCNc1ccn(C2OC(COP(=O)(O)OCC3OC(…`

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
ZINC316109	1.000	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NC[C@H]2CCCO2)cc1`
ZINC316110	1.000	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NC[C@@H]2CCCO2)cc1`
ZINC3286414	1.000	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)cc1`
ZINC3286415	1.000	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)cc1`
ZINC3860453	1.000	332.3 Da LogP 3.67 TPSA 76.0	✓ Ro5	✓ Clean	`O=C1OC2(c3ccc(O)cc3Oc3cc(O)ccc32)c2ccccc21`
ZINC46867	1.000	226.3 Da LogP 1.80 TPSA 50.4	✓ Ro5	✓ Clean	`O=C(NC[C@H]1CCCO1)NC1CCCCC1`
ZINC46868	1.000	226.3 Da LogP 1.80 TPSA 50.4	✓ Ro5	✓ Clean	`O=C(NC[C@@H]1CCCO1)NC1CCCCC1`
ZINC798668	1.000	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NC[C@H]1CCCO1`
ZINC798669	1.000	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NC[C@@H]1CCC…`
ZINC804908	0.979	382.5 Da LogP 1.58 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCC2)cc1)NC[C@H]1CCCO1`
ZINC804909	0.979	382.5 Da LogP 1.58 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCC2)cc1)NC[C@@H]1CCCO1`
ZINC30984714	0.968	212.3 Da LogP 1.41 TPSA 50.4	✓ Ro5	✓ Clean	`O=C(NC[C@@H]1CCCO1)NC1CCCC1`
ZINC30984716	0.968	212.3 Da LogP 1.41 TPSA 50.4	✓ Ro5	✓ Clean	`O=C(NC[C@H]1CCCO1)NC1CCCC1`
ZINC3485814	0.870	366.9 Da LogP 2.52 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(Cl)cc1`
ZINC3485816	0.870	366.9 Da LogP 2.52 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(Cl)cc1`
ZINC6914139	0.870	350.4 Da LogP 2.01 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(F)cc1`
ZINC6914143	0.870	350.4 Da LogP 2.01 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(F)cc1`
ZINC12360002	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC3402375	0.855	388.5 Da LogP 3.17 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(C(C)(C)C)c…`
ZINC3402380	0.855	388.5 Da LogP 3.17 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(C(C)(C)C)…`
ZINC4806433	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC43199396	0.842	331.3 Da LogP 3.54 TPSA 81.8	✓ Ro5	✓ Clean	`Nc1ccc2c(c1)Oc1cc(O)ccc1[C@]21OC(=O)c2ccccc21`
ZINC43199397	0.842	331.3 Da LogP 3.54 TPSA 81.8	✓ Ro5	✓ Clean	`Nc1ccc2c(c1)Oc1cc(O)ccc1[C@@]21OC(=O)c2ccccc21`
ZINC880963	0.839	362.5 Da LogP 1.88 TPSA 78.3	✓ Ro5	✓ Clean	`COc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)cc1`
ZINC880965	0.839	362.5 Da LogP 1.88 TPSA 78.3	✓ Ro5	✓ Clean	`COc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)cc1`
ZINC26662657	0.833	254.2 Da LogP -0.59 TPSA 93.3	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3cncnc32)[C@@H](F)[C@@H]1O`
ZINC2207000	0.810	403.5 Da LogP 2.22 TPSA 98.1	✓ Ro5	✓ Clean	`CCC(=O)Nc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)c…`
ZINC2207001	0.810	403.5 Da LogP 2.22 TPSA 98.1	✓ Ro5	✓ Clean	`CCC(=O)Nc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)…`
ZINC62065644	0.800	228.3 Da LogP 0.64 TPSA 59.6	✓ Ro5	✓ Clean	`O=C(NC[C@H]1CCCO1)NC1CCOCC1`
ZINC62065645	0.800	228.3 Da LogP 0.64 TPSA 59.6	✓ Ro5	✓ Clean	`O=C(NC[C@@H]1CCCO1)NC1CCOCC1`
ZINC212148859	0.791	254.2 Da LogP -0.59 TPSA 93.3	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3cncnc32)[C@H](O)[C@@H]1F`
ZINC13518964	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1571045	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC2046931	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](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.