Protein profile

VK055_2094

htpG

Genome: KpATCC43816

Gene: AIK80699.1 htpG Structure source: AlphaFold + ColabFold UniProt A0A0H3GSX3

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Amino acids 624

Annotations 6

Features 47

PDB binders 28

Druggability 0.501

Overview

Basic information about this protein and its source genome.

Accession: VK055_2094
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: AIK80699.1 htpG
Status: annotated
Amino acids: 624
Structure source: AlphaFold + ColabFold

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0006457 The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. GO:0140662 Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. GO:0051082 Binding to an unfolded protein. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 65.789
Human E-value: 2.16e-10
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 93.429
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 89.25

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 A0A0H3GSX3

Pocket Pocket 27

P2Rank 0.867

Structure A0A0H3GSX3

Pocket Pocket 1

ColabFold model

FPocket 0.467 · Pocket 3

P2Rank 0.888 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 227 / 4744 genomes with a hit

Normalized 0.048

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0006457 The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
GO:0140662 Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GO:0051082 Binding to an unfolded protein.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Sequence Features

Domain/signature hits from InterPro and related databases.

47 records

Show feature table

Start	End	DB	Term	Name
27	184	SMART	SM00387	HKATPase_4
27	184	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
229	396	FunFam	G3DSA:3.30.230.80:FF:000002	Molecular chaperone HtpG
1	220	FunFam	G3DSA:3.30.565.10:FF:000009	Molecular chaperone HtpG
1	624	PIRSF	PIRSF002583	HSP90_HTPG
1	624	InterPro	IPR001404	Heat shock protein Hsp90 family
25	34	ProSitePatterns	PS00298	Heat shock hsp90 proteins family signature.
25	34	InterPro	IPR019805	Heat shock protein Hsp90, conserved site
510	622	SUPERFAMILY	SSF110942	HSP90 C-terminal domain
510	622	InterPro	IPR037196	HSP90, C-terminal domain
14	204	CDD	cd16927	HATPase_Hsp90-like
14	204	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
93	110	PRINTS	PR00775	90kDa heat shock protein signature
93	110	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
120	142	PRINTS	PR00775	90kDa heat shock protein signature
120	142	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
26	48	PRINTS	PR00775	90kDa heat shock protein signature
26	48	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
190	208	PRINTS	PR00775	90kDa heat shock protein signature
190	208	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
172	189	PRINTS	PR00775	90kDa heat shock protein signature
172	189	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
75	92	PRINTS	PR00775	90kDa heat shock protein signature
75	92	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
5	25	PRINTS	PR00775	90kDa heat shock protein signature
5	25	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
483	503	Coils	Coil	Coil
211	623	Pfam	PF00183	Hsp90 protein
211	623	InterPro	IPR001404	Heat shock protein Hsp90 family
491	623	Gene3D	G3DSA:1.20.120.790	-
491	623	InterPro	IPR037196	HSP90, C-terminal domain
1	215	Gene3D	G3DSA:3.30.565.10	-
1	215	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
229	396	Gene3D	G3DSA:3.30.230.80	-
4	213	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
4	213	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
5	622	PANTHER	PTHR11528	HEAT SHOCK PROTEIN 90 FAMILY MEMBER
5	622	InterPro	IPR001404	Heat shock protein Hsp90 family
27	182	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
27	182	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
397	489	FunFam	G3DSA:3.40.50.11260:FF:000002	Molecular chaperone HtpG
397	489	Gene3D	G3DSA:3.40.50.11260	-
491	624	FunFam	G3DSA:1.20.120.790:FF:000002	Molecular chaperone HtpG
230	485	SUPERFAMILY	SSF54211	Ribosomal protein S5 domain 2-like
230	485	InterPro	IPR020568	Ribosomal protein S5 domain 2-type fold
2	623	Hamap	MF_00505	Chaperone protein HtpG [htpG].
2	623	InterPro	IPR001404	Heat shock protein Hsp90 family

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_A0A0H3GSX3	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_2094	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
27				0.501
39				0.305
60				0.253

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	11.56	0.616
2	9.61	0.517
3	5.59	0.268
4	4.65	0.202
5	3.92	0.154

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
3				0.467
33				0.207

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	12.41	0.65
2	10.36	0.557
3	5.21	0.242
4	3.28	0.115
5	1.66	0.028

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.

84 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
13C	2XX2	P02829	337.8 Da LogP 3.11 TPSA 86.6	✓ Ro5	✓ Clean	`c1c(c2c(c(c1O)Cl)CC(=O)CCCCC=CCCNC2=O)O`
13I	2XX4	P02829	411.9 Da LogP 2.69 TPSA 116.1	✓ Ro5	✓ Clean	`CCO[C@H]([C@H]1CCC\C=C\CCNC(=O)c2c(cc(c(c2CC1=O…`
13N	2XX5	P02829	471.0 Da LogP 3.66 TPSA 115.7	✓ Ro5	✓ Clean	`c1ccc(cc1)CNC(=O)[C@@H]2CCC\C=C\CCNC(=O)c3c(cc(…`
2GJ	7K9S	J9VVA4	465.6 Da LogP 4.13 TPSA 108.1	✓ Ro5	✓ Clean	`CCNC(=O)c1c(c(on1)c2cc(c(cc2O)O)C(C)C)c3ccc(cc3…`
4QS	4AS9	P02829	574.7 Da LogP 2.80 TPSA 163.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@@H](C=C([C@H]([C@H](/C…`
59C	4ASA	P02829	599.7 Da LogP 2.93 TPSA 166.3	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@@H](C=C([C@H]([C@H](/C…`
62U	4ASF	P02829	626.7 Da LogP 3.53 TPSA 176.6	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H](C(C=C([C@H]([C@H](C=CC=C(…`
7FK	4CE1	P02829	379.9 Da LogP 4.24 TPSA 77.8	✓ Ro5	✓ Clean	`CN1CC/C=C/CCCCCCC(=O)Cc2c(c(cc(c2Cl)O)O)C1=O`
814	4ASG	P02829	636.7 Da LogP 3.94 TPSA 163.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@@H](C=C(C([C@H](/C=C\C…`
8TO	4ASB	P02829	630.8 Da LogP 2.30 TPSA 169.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@@H](C=C([C@H]([C@H](C=…`
ACP	4XC0	P54651	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
AGS	6XLH	P15108	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	6XLC	P15108	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)…`
BC6	2VW5	P02829	502.7 Da LogP 4.70 TPSA 131.1	1 viol.	✓ Clean	`C[C@H]1CC\C=C(\C(=O)Nc2cc(cc(c2)O)C[C@H](C[C@@H…`
BO5	4CE2	P02829	365.9 Da LogP 3.85 TPSA 77.8	✓ Ro5	✓ Clean	`CN1CC/C=C/CCCCCC(=O)Cc2c(c(cc(c2Cl)O)O)C1=O`
D1S	3Q5J	Q4Q4I6	630.8 Da LogP 2.30 TPSA 169.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@H](/C=C(/[C@@H]([C@H](…`
D1U	3Q5K	Q4Q4I6	440.5 Da LogP 3.92 TPSA 90.0	✓ Ro5	✓ Clean	`CC1(Cc2c(c(nn2c3ccc(c(c3)NCCSC)C(=O)N)C(F)(F)F)…`
GDM	4XDM	P54651	560.6 Da LogP 2.41 TPSA 163.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@H](\C=C(\[C@@H]([C@H](…`
H64	1ZW9	P02829	465.4 Da LogP 3.44 TPSA 100.1	✓ Ro5	✓ Clean	`CC(C)NCCCn1c2c(c(ncn2)N)nc1Sc3cc4c(cc3Br)OCO4`
KX2	3Q5L	Q4Q4I6	642.8 Da LogP 2.45 TPSA 169.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@H](/C=C(/[C@@H]([C@H](…`
L4V	4CE3	P02829	351.8 Da LogP 3.46 TPSA 77.8	✓ Ro5	✓ Clean	`CN1CCC/C=C\CCCC(=O)Cc2c(c(cc(c2Cl)O)O)C1=O`
RDA	2FXS	P02829	411.8 Da LogP 2.53 TPSA 145.6	✓ Ro5	✓ Clean	`COc1cc(c(cc1O)NC(=O)CCc2c(c(cc(c2Cl)O)O)C(=O)OC…`
RDE	1ZWH	P02829	397.8 Da LogP 2.76 TPSA 120.5	✓ Ro5	✓ Clean	`COc1cc(c(c(c1OC)CCOC(=O)c2cc(c(cc2O)O)Cl)OC)N`
TAM	4XKA	P54651	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`
W8S	7K9W	J9VVA4	456.5 Da LogP 4.41 TPSA 99.9	✓ Ro5	✓ Clean	`Cn1c(cc(n1)c2cccc(c2)OC)Nc3cc(cc(c3C(=O)N4Cc5cc…`
W8V	7K9V	J9VVA4	440.5 Da LogP 4.71 TPSA 90.6	✓ Ro5	✓ Clean	`Cc1ccccc1c2cc(n(n2)C)Nc3cc(cc(c3C(=O)N4Cc5ccccc…`
W8Y	7K9U	J9VVA4	427.5 Da LogP 3.79 TPSA 103.5	✓ Ro5	✓ Clean	`Cn1c(cc(n1)c2ccccc2)Nc3cc(cc(c3C(=O)N4Cc5cccnc5…`
XD6	2XD6	P02829	366.8 Da LogP 3.11 TPSA 100.9	✓ Ro5	✓ Clean	`c1c(c2c(c(c1O)Cl)CC(=O)CCCC/C(=C/CCOC2=O)/C=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL424811	P15108	6.96	373.8 Da LogP 3.18 TPSA 107.5	✓ Ro5	✓ Clean	`CNC(=O)c1[nH]nc(-c2cc(Cl)c(O)cc2O)c1-c1ccc(OC)c…`
BSM	P15108	6.85	387.8 Da LogP 3.57 TPSA 107.5	✓ Ro5	✓ Clean	`CCNC(=O)c1c(c([nH]n1)c2cc(c(cc2O)O)Cl)c3ccc(cc3…`
RDC	P15108	6.70	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2[C@H](O2)\C=C/C=C/C(=O)Cc3c(c(c…`
CHEMBL190182	P15108	6.41	432.3 Da LogP 3.68 TPSA 107.5	✓ Ro5	✓ Clean	`CCNC(=O)c1[nH]nc(-c2cc(Br)c(O)cc2O)c1-c1ccc(OC)…`
CHEMBL366215	P15108	6.38	359.8 Da LogP 2.92 TPSA 121.5	✓ Ro5	✓ Clean	`COc1ccc(-c2c(-c3cc(Cl)c(O)cc3O)n[nH]c2C(N)=O)cc1`
CHEMBL191074	P15108	6.19	358.8 Da LogP 3.89 TPSA 87.6	✓ Ro5	✓ Clean	`Cc1[nH]nc(-c2cc(Cl)c(O)cc2O)c1-c1ccc2c(c1)OCCO2`

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
ZINC100006925	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C\C=C/C(=O)Cc2c(Cl)c(…`
ZINC100013319	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(O…`
ZINC100013323	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@H]1C[C@H]2O[C@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(O)…`
ZINC100015656	1.000	465.6 Da LogP 4.13 TPSA 108.1	✓ Ro5	✓ Clean	`CCNC(=O)c1noc(-c2cc(C(C)C)c(O)cc2O)c1-c1ccc(CN2…`
ZINC100152234	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C/C=C/C(=O)Cc2c(Cl)c(…`
ZINC13521629	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C\C=C\C(=O)Cc2c(Cl)c(…`
ZINC2061000778	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@H]1C[C@@H]2O[C@H]2C=CC=CC(=O)Cc2c(Cl)c(O)cc…`
ZINC253952046	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2O[C@H]2C=CC=CC(=O)Cc2c(Cl)c(O)c…`
ZINC253987424	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2C=CC=CC(=O)Cc2c(Cl)c(O)c…`
ZINC253987427	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@H]2C=CC=CC(=O)Cc2c(Cl)c(O)cc…`
ZINC253987428	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2O[C@@H]2C=CC=CC(=O)Cc2c(Cl)c(O)…`
ZINC33838895	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@H]2/C=C\C=C/C(=O)Cc2c(Cl)c(O…`
ZINC45789132	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(…`
ZINC45789135	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@H]1C[C@H]2O[C@@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(O…`
ZINC5492965	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2O[C@H]2/C=C\C=C\C(=O)Cc2c(Cl)c(…`
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)…`
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(=…`
ZINC4617893	0.796	387.8 Da LogP 3.57 TPSA 107.5	✓ Ro5	✓ Clean	`CCNC(=O)c1[nH]nc(-c2cc(Cl)c(O)cc2O)c1-c1ccc(OC)…`
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](…`
ZINC1532515	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…`
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]…`
ZINC1842158	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…`
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…`
ZINC8613167	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…`
ZINC4096224	0.768	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC238855217	0.750	560.6 Da LogP 2.41 TPSA 163.5	1 viol.	Alert	`COC1=C2C[C@@H](C)C[C@H](OC)[C@H](O)[C@@H](C)/C=…`

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.