Protein profile

KP13_03016

putative ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter

Genome: KpKP13

Gene: AHE45600.1 Structure source: AlphaFold + ColabFold UniProt A0A6A8EFY1

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Amino acids 895

Annotations 14

Features 81

PDB binders 27

Druggability 0.811

Overview

Basic information about this protein and its source genome.

Accession: KP13_03016
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE45600.1
Status: annotated
Amino acids: 895
Structure source: AlphaFold + ColabFold

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:0005215 Enables the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, accross or in between cells. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. 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:0012505 A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 45.669
Human E-value: 2.17e-25
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 87.81

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 0.811

Structure A0A6A8EFY1

Pocket Pocket 3

P2Rank 0.69

Structure A0A6A8EFY1

Pocket Pocket 1

ColabFold model

FPocket 0.842 · Pocket 9

P2Rank 0.694 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 49 / 4744 genomes with a hit

Normalized 0.01

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

14 GO

Gene Ontology (GO)

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:0005215 Enables the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, accross or in between cells.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
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:0012505 A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0046872 Binding to a metal ion.
GO:0005391 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) + K+(out) = ADP + phosphate + Na+(out) + K+(in).
GO:0030007 A homeostatic process involved in the maintenance of a steady state level of potassium ions within a cell.
GO:0006883 A homeostatic process involved in the maintenance of a steady state level of sodium ions within a cell.
GO:1990573 The directed movement of potassium ions from outside of a cell, across the plasma membrane and into the cytosol.
GO:1902600 The directed movement of a proton across a membrane.
GO:0036376 The directed movement of sodium ions from inside of a cell, across the plasma membrane and into the extracellular region.

Sequence Features

Domain/signature hits from InterPro and related databases.

81 records

Show feature table

Start	End	DB	Term	Name
312	685	SFLD	SFLDF00027	p-type atpase
312	685	InterPro	IPR044492	P-type ATPase, haloacid dehalogenase domain
1	53	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
328	735	SUPERFAMILY	SSF56784	HAD-like
328	735	InterPro	IPR036412	HAD-like superfamily
28	230	Gene3D	G3DSA:2.70.150.10	-
249	268	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
309	692	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
10	76	Pfam	PF00690	Cation transporter/ATPase, N-terminus
10	76	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
745	764	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
527	677	FunFam	G3DSA:3.40.50.1000:FF:000028	Calcium-transporting P-type ATPase, putative
326	646	Pfam	PF00702	haloacid dehalogenase-like hydrolase
885	895	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
246	268	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
604	620	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
604	620	InterPro	IPR001757	P-type ATPase
632	648	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
632	648	InterPro	IPR001757	P-type ATPase
664	689	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
664	689	InterPro	IPR001757	P-type ATPase
489	507	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
489	507	InterPro	IPR001757	P-type ATPase
531	542	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
553	563	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
656	668	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
632	651	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
330	344	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
167	181	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
718	722	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
54	76	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
88	351	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
88	351	InterPro	IPR001757	P-type ATPase
601	725	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
601	725	InterPro	IPR001757	P-type ATPase
719	741	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
865	884	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
269	279	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
103	248	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
312	685	SFLD	SFLDG00002	C1.7: P-type atpase like
764	786	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
80	102	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
828	850	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
717	886	Pfam	PF00689	Cation transporting ATPase, C-terminus
717	886	InterPro	IPR006068	Cation-transporting P-type ATPase, C-terminal
854	864	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
795	814	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
327	677	Gene3D	G3DSA:3.40.50.1000	-
327	677	InterPro	IPR023214	HAD superfamily
15	874	PANTHER	PTHR42861	CALCIUM-TRANSPORTING ATPASE
104	230	FunFam	G3DSA:2.70.150.10:FF:000160	Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
77	81	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
120	229	SUPERFAMILY	SSF81653	Calcium ATPase, transduction domain A
120	229	InterPro	IPR008250	P-type ATPase, A domain superfamily
784	794	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
9	893	SUPERFAMILY	SSF81665	Calcium ATPase, transmembrane domain M
9	893	InterPro	IPR023298	P-type ATPase, transmembrane domain superfamily
815	833	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
796	815	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
60	890	Gene3D	G3DSA:1.20.1110.10	-
693	717	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
332	338	ProSitePatterns	PS00154	E1-E2 ATPases phosphorylation site.
332	338	InterPro	IPR018303	P-type ATPase, phosphorylation site
327	339	FunFam	G3DSA:3.40.50.1000:FF:000001	Phospholipid-transporting ATPase IC
723	744	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
280	308	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
834	853	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
765	783	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
865	884	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
54	76	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
117	310	Pfam	PF00122	E1-E2 ATPase
340	538	Gene3D	G3DSA:3.40.1110.10	-
340	538	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
337	535	SUPERFAMILY	SSF81660	Metal cation-transporting ATPase, ATP-binding domain N
337	535	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
692	714	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
9	82	SMART	SM00831	Cation_ATPase_N_a_2
9	82	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
28	886	CDD	cd02080	P-type_ATPase_cation
82	102	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
283	305	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.

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_A0A6A8EFY1	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03016	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
3				0.811
6				0.235

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	8.99	0.481
2	8.67	0.463
3	6.46	0.326
4	5.26	0.246
5	3.84	0.15

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
9				0.842
24				0.645
35				0.437
48				0.273

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	7.57	0.399
2	6.91	0.356
3	5.04	0.229
4	4.38	0.184
5	4.37	0.183

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.

107 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
128	5A3S	P04191-2	718.3 Da LogP -1.20 TPSA 389.7	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@H]4[C@@H]([C@H](O3)C…`
12D	3AR6	P04191-2	638.3 Da LogP -1.01 TPSA 340.0	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@H]4[C@@H]([C@H](O3)C…`
1HT	4J2T	P04191-2	720.9 Da LogP 5.28 TPSA 178.0	3 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C([C@@H]1OC(=O)C(=C…`
7BL	4YCN	P04191-2	428.6 Da LogP 6.01 TPSA 55.8	1 viol.	✓ Clean	`C/C=C/C/C(=C\[C@H]1C/C=C/C=C/C[C@@H](/C=C(/[C@H…`
7BS	4YCM	P04191-2	604.8 Da LogP 4.49 TPSA 123.9	1 viol.	✓ Clean	`C/C=C/C/C(=C\[C@H]1C/C=C/C=C/C[C@@H](/C=C(/[C@H…`
8T8	5NCQ	P04191-2	439.3 Da LogP 6.00 TPSA 37.0	1 viol.	Alert	`c1cc(ccc1CN[C@H]2CCCc3c2[nH]c4c3ccc(c4)OC(F)(F)…`
9TN	2YFY	P04191-2	580.7 Da LogP 2.58 TPSA 165.9	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C([C@@H]1OC(=O)/C(=…`
ACP	3B9R	P04191-2	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)…`
ALF	1XP5	P04191-2	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
AN2	3BA6	P04191-2	426.2 Da LogP -1.78 TPSA 238.4	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BEF	2ZBE	P04191-2	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
BHQ	2AGV	P04191-2	222.3 Da LogP 3.69 TPSA 40.5	✓ Ro5	✓ Clean	`CC(C)(C)c1cc(c(cc1O)C(C)(C)C)O`
CZA	4BEW	P04191	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`CC(=O)C1=C(N2[C@H](C1=O)[C@H]3c4c[nH]c5c4c(ccc5…`
DBK	3NAL	B6CAM1	620.8 Da LogP 5.17 TPSA 145.7	2 viol.	✓ Clean	`CCCCCCCCCCCC(=O)O[C@H]1C[C@]([C@H]2C[C@H](C(=C2…`
DL5	5A3Q	P04191-2	716.3 Da LogP -1.08 TPSA 380.5	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@H]4[C@@H]([C@H](O3)C…`
DMU	5ZMW	P04191-2	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)C…`
HZ1	3NAN	B6CAM1	944.2 Da LogP 7.42 TPSA 230.5	3 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C([C@H]3[C@]([C@H](C[C…`
MF4	1WPG	P04191-2	100.3 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Mg-2](F)(F)F`
MGF	4BEW	P04191	81.3 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Mg-](F)F`
OHW	6YAA	P04191-2	439.5 Da LogP 4.88 TPSA 40.7	✓ Ro5	Alert	`CCCc1c2ccc(cc2[nH]c1[C@H]3CCCCN3CCN4CCOCC4)OC(F…`
OTK	3NAM	B6CAM1	510.6 Da LogP 1.98 TPSA 145.7	1 viol.	✓ Clean	`CCCC(=O)O[C@H]1C[C@]([C@H]2C[C@H]([C@@H]([C@H]2…`
PC1	2ZBD	P04191-2	790.2 Da LogP 12.17 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)([O-])…`
PCW	4UU1	P04191-2	787.1 Da LogP 12.36 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)…`
PTY	2AGV	P04191-2	734.1 Da LogP 11.67 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCCCC…`
TBU	4UU0	P04191-2	74.1 Da LogP 0.78 TPSA 20.2	✓ Ro5	✓ Clean	`CC(C)(C)O`
TM1	3AR8	P04191-2	558.3 Da LogP -1.12 TPSA 293.5	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@H]4[C@@H]([C@H](O3)C…`
VN4	5A3Q	P04191-2	98.9 Da LogP -1.43 TPSA 57.2	✓ Ro5	✓ Clean	`[O-][V](=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
TG1	P04191	9.70	650.8 Da LogP 3.93 TPSA 172.0	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C([C@@H]1OC(=O)/C(=…`
CHEMBL1253591	P04191	9.10	672.8 Da LogP 4.28 TPSA 172.0	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C(C)[C@@H]1OC(=O)c1…`
CHEMBL1253563	P04191	8.82	628.7 Da LogP 2.88 TPSA 172.0	2 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL2332551	P04191	8.77	675.8 Da LogP 5.18 TPSA 156.3	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253557	P04191	8.60	678.8 Da LogP 4.71 TPSA 172.0	2 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253558	P04191	8.60	734.9 Da LogP 6.27 TPSA 172.0	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL2332104	P04191	8.59	692.8 Da LogP 4.50 TPSA 178.0	2 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253594	P04191	8.52	748.9 Da LogP 5.94 TPSA 172.0	3 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C(C)[C@@H]1OC(=O)c1…`
CHEMBL2332101	P04191	8.07	748.9 Da LogP 6.06 TPSA 178.0	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253592	P04191	8.05	686.8 Da LogP 4.58 TPSA 172.0	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C(C)[C@@H]1OC(=O)c1…`
CHEMBL2332105	P04191	8.03	736.9 Da LogP 4.86 TPSA 187.3	2 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253562	P04191	8.00	580.7 Da LogP 2.58 TPSA 165.9	2 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253589	P04191	7.96	748.9 Da LogP 6.06 TPSA 178.0	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL2332100	P04191	7.96	720.9 Da LogP 5.28 TPSA 178.0	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL4534285	P04191	7.96	650.8 Da LogP 3.93 TPSA 172.0	2 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL2332102	P04191	7.89	720.9 Da LogP 5.13 TPSA 178.0	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL2332554	P04191	7.89	632.7 Da LogP 4.97 TPSA 144.0	2 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253559	P04191	7.81	712.8 Da LogP 5.22 TPSA 172.0	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253593	P04191	7.75	762.9 Da LogP 5.87 TPSA 172.0	3 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C(C)[C@@H]1OC(=O)Cc…`
CHEMBL4514624	P04191	7.75	622.8 Da LogP 3.24 TPSA 142.4	2 viol.	✓ Clean	`C/C=C/C/C(C)=C\[C@@H]1OC(=O)C[C@H](O[C@@H]2O[C@…`
CHEMBL5268892	P04191	7.75	636.8 Da LogP 3.63 TPSA 142.4	2 viol.	✓ Clean	`C/C=C/C/C(C)=C\[C@H]1C[C@H]2C=C[C@H](C[C@H](C)/…`
CHEMBL1253588	P04191	7.72	648.8 Da LogP 5.16 TPSA 143.9	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253555	P04191	7.70	608.7 Da LogP 3.36 TPSA 165.9	2 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253556	P04191	7.70	664.8 Da LogP 4.92 TPSA 165.9	2 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL2332552	P04191	7.70	703.9 Da LogP 5.96 TPSA 156.3	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253561	P04191	7.57	803.0 Da LogP 6.82 TPSA 172.0	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL1253595	P04191	7.36	686.8 Da LogP 4.58 TPSA 172.0	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C(C)[C@@H]1OC(=O)c1…`
CHEMBL2332103	P04191	7.26	777.0 Da LogP 6.84 TPSA 178.0	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL2332553	P04191	7.10	733.9 Da LogP 5.59 TPSA 165.5	3 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`
CHEMBL468766	P04191	7.05	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`C/C(O)=C1\C(=O)[C@@H]2[C@H]3c4c[nH]c5cccc(c45)C…`

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
ZINC100053689	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC100053691	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC102190506	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC1501015302	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC2039285652	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285653	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285654	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285655	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2053493146	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493147	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493148	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493149	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC238809244	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC238809245	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC252695223	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695224	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695225	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695226	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC29084193	1.000	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`CC(=O)C1=C(O)N2[C@H](C1=O)[C@H]1c3c[nH]c4cccc(c…`
ZINC56404	1.000	222.3 Da LogP 3.69 TPSA 40.5	✓ Ro5	✓ Clean	`CC(C)(C)c1cc(O)c(C(C)(C)C)cc1O`
ZINC58649715	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC59978443	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](…`
ZINC66157001	1.000	468.5 Da LogP -1.62 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC70669940	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669941	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669942	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669943	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC77311968	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H]…`
ZINC83433913	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](CO…`
ZINC85482724	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC86002923	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@H](O[C@H]2O[C@H](CO)…`
ZINC27416437	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC13544781	0.880	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783	0.880	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC105469665	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC13543439	0.860	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543441	0.860	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC12503599	0.839	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	0.839	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	0.839	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	0.839	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	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`

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.