Protein target profile

PA4407

cell division protein FtsZ

Genome: NC_002516.2

Gene: ftsZ PA4407 3D evidence: Experimental + AlphaFold DB model UniProt P47204

Export view

Length 394

Pocket druggability 0.694

Ligand records 79

EC / GO 0 / 8

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

4 signals

Strengths

Risks / watch

No major risk signal surfaced in the loaded evidence.

Missing evidence

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

How to read 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 TPW 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.

Overview

Basic information about this protein and its source genome.

Accession: PA4407
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: ftsZ PA4407
Status: annotated
Amino acids: 394
3D evidence: Experimental + AlphaFold DB model

GO:0032153 The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005525 Binding to GTP, guanosine triphosphate. GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. GO:0000917 The assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis. The progeny cells that form a division septum are not able to exchange intracellular material.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: Hit
Essential (DEG): Y
Localization: Cytoplasmic

Selected pocket evidence

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.694

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MFELVDNIAQTAVIKVIGVGGGGGNAVNHMAKNNVEGVEFICANTDAQALKNIAARTVLQLGPGVTKGLGAGANPEVGRQAALEDRERISEVLEGADMVFITTGMGGGTGTGAAPIIAEVAKEMGILTVAVVTRPFPFEGRKRMQIADEGIRALAESVDSLITIPNEKLLTILGKDASLLAAFAKADDVLAGAVRGISDIIKRPGMINVDFADVKTVMSEMGMAMMGTGCASGPNRAREATEAAIRNPLLEDVNLQGARGILVNITAGPDLSLGEYSDVGNIIEQFASEHATVKVGTVIDADMRDELHVTVVATGLGARLEKPVKVVDNTVQGSAAQAAAPAQREQQSVNYRDLDRPTVMRNQSHGSAATAAKLNPQDDLDYLDIPAFLRRQAD

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

GO:0032153 The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005525 Binding to GTP, guanosine triphosphate.
GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
GO:0000917 The assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis. The progeny cells that form a division septum are not able to exchange intracellular material.
GO:0043093 A cytokinesis process that involves a set of conserved proteins including FtsZ, and results in the formation of two similarly sized and shaped cells.
GO:0051258 The process of creating protein polymers, compounds composed of a large number of component monomers; polymeric proteins may be made up of different or identical monomers. Polymerization occurs by the addition of extra monomers to an existing poly- or oligomeric protein.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
225	320	Gene3D	G3DSA:3.30.1330.20	-
225	320	InterPro	IPR037103	Tubulin/FtsZ-like, C-terminal domain
98	118	PRINTS	PR00423	Cell division protein FtsZ signature
98	118	InterPro	IPR003008	Tubulin/FtsZ, GTPase domain
189	211	PRINTS	PR00423	Cell division protein FtsZ signature
189	211	InterPro	IPR003008	Tubulin/FtsZ, GTPase domain
212	233	PRINTS	PR00423	Cell division protein FtsZ signature
212	233	InterPro	IPR003008	Tubulin/FtsZ, GTPase domain
126	147	PRINTS	PR00423	Cell division protein FtsZ signature
126	147	InterPro	IPR003008	Tubulin/FtsZ, GTPase domain
225	347	FunFam	G3DSA:3.30.1330.20:FF:000004	Cell division protein FtsZ
14	173	Pfam	PF00091	Tubulin/FtsZ family, GTPase domain
14	173	InterPro	IPR003008	Tubulin/FtsZ, GTPase domain
9	328	NCBIfam	TIGR00065	cell division protein FtsZ
9	328	InterPro	IPR000158	Cell division protein FtsZ
44	78	ProSitePatterns	PS01134	FtsZ protein signature 1.
44	78	InterPro	IPR020805	Cell division protein FtsZ, conserved site
207	325	SMART	SM00865	Tubulin_C_4
207	325	InterPro	IPR018316	Tubulin/FtsZ, 2-layer sandwich domain
9	366	Hamap	MF_00909	Cell division protein FtsZ [ftsZ].
9	366	InterPro	IPR000158	Cell division protein FtsZ
97	118	ProSitePatterns	PS01135	FtsZ protein signature 2.
97	118	InterPro	IPR020805	Cell division protein FtsZ, conserved site
3	220	Gene3D	G3DSA:3.40.50.1440	Tubulin/FtsZ, GTPase domain
3	220	InterPro	IPR036525	Tubulin/FtsZ, GTPase domain superfamily
13	208	SUPERFAMILY	SSF52490	Tubulin nucleotide-binding domain-like
13	208	InterPro	IPR036525	Tubulin/FtsZ, GTPase domain superfamily
204	319	SUPERFAMILY	SSF55307	Tubulin C-terminal domain-like
204	319	InterPro	IPR008280	Tubulin/FtsZ, C-terminal
9	323	PANTHER	PTHR30314	CELL DIVISION PROTEIN FTSZ-RELATED
9	323	InterPro	IPR045061	Tubulin-like protein FtsZ/CetZ
13	205	SMART	SM00864	Tubulin_4
13	205	InterPro	IPR003008	Tubulin/FtsZ, GTPase domain
25	315	CDD	cd02201	FtsZ_type1
25	315	InterPro	IPR000158	Cell division protein FtsZ
11	317	FunFam	G3DSA:3.40.50.1440:FF:000023	Cell division protein FtsZ
222	316	Pfam	PF12327	FtsZ family, C-terminal domain
222	316	InterPro	IPR024757	Cell division protein FtsZ, C-terminal

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.

Loading 3D structure...

Legend High Medium Low

Structural evidence

2 + 1

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
PDB 2VAW	X-ray	2.90 Å	A	100.0% 1-394	PDBe RCSB PDBj File	Viewing
PDB 1OFU	X-ray	2.10 Å	A,B	81.2% 1-320	PDBe RCSB PDBj File	Loaded
AlphaFold DB PA4407	AlphaFold DB	—	—	full sequence	—	Loaded

Pocket details Inspect a specific pocket, or open the full viewer

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.

79 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 79 via homologs

Structural ligands 2 0 loaded crystals

Bioactive compounds 27 50 ZINC proposed compounds

Drug-like & clean 36 13 PAINS alerts

Best available ligand signal

GSP PDB via homolog 539.2 Da · LogP -2.22 · TPSA 282.0 Open detail RCSB PDB

Detail RCSB PDB GSP PDB via homolog

Detail RCSB PDB MB3 PDB via homolog

Detail ChEMBL CHEMBL5085404 ChEMBL via homolog · pchembl 6.70

Detail ChEMBL CHEMBL5080731 ChEMBL via homolog · pchembl 6.16

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
GSP RCSB PDB	3WGN	P0A029	539.2 Da LogP -2.22 TPSA 282.0	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
MB3 RCSB PDB	6RVP	P0A031	99.1 Da LogP 0.24 TPSA 20.3	✓ Ro5	✓ Clean	`CN1CCCC1=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
CHEMBL5085404 ChEMBL	A5Z1V5	6.70	402.4 Da LogP 4.74 TPSA 64.3	✓ Ro5	✓ Clean	`CCC[C@H](COc1ccc(F)c(C(N)=O)c1F)Nc1cccc(C(F)(F)…`
CHEMBL5080731 ChEMBL	A5Z1V5	6.16	331.2 Da LogP 3.66 TPSA 52.3	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OCc2cccc(C(F)(F)F)c2)c1F`
3MB ChEMBL	P0A031	—	151.2 Da LogP 0.79 TPSA 52.3	✓ Ro5	✓ Clean	`COc1cccc(c1)C(=O)N`
9PC ChEMBL	P17865	—	355.8 Da LogP 3.30 TPSA 78.1	✓ Ro5	✓ Clean	`c1cc(c(c(c1OCc2nc3cc(cnc3s2)Cl)F)C(=O)N)F`
9TF ChEMBL	A5Z1V5	—	256.2 Da LogP 1.58 TPSA 94.8	✓ Ro5	Alert	`c1ccc2c(c1)C(=O)c3c(cc(c(c3C2=O)O)O)O`
CHEMBL1095212 ChEMBL	P0A031	—	306.3 Da LogP 3.47 TPSA 65.2	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(Oc2nc3ccccc3s2)c1F`
CHEMBL1095809 ChEMBL	P0A031	—	334.3 Da LogP 3.56 TPSA 65.2	✓ Ro5	✓ Clean	`Cc1ccc2nc(COc3ccc(F)c(C(N)=O)c3F)sc2c1`
CHEMBL1096128 ChEMBL	P0A031	—	396.4 Da LogP 4.92 TPSA 65.2	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OCc2nc3ccc(-c4ccccc4)cc3s2)c1F`
CHEMBL1096989 ChEMBL	P0A031	—	350.3 Da LogP 3.26 TPSA 74.4	✓ Ro5	✓ Clean	`COc1ccc2nc(COc3ccc(F)c(C(N)=O)c3F)sc2c1`
CHEMBL1097096 ChEMBL	P0A031	—	396.4 Da LogP 4.92 TPSA 65.2	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OCc2nc3cccc(-c4ccccc4)c3s2)c1F`
CHEMBL1097101 ChEMBL	P0A031	—	396.4 Da LogP 4.92 TPSA 65.2	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OCc2nc3c(-c4ccccc4)cccc3s2)c1F`
CHEMBL1097435 ChEMBL	P0A031	—	386.4 Da LogP 3.64 TPSA 93.9	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OCc2nc3cc(-c4ncc[nH]4)ccc3s2)c1F`
CHEMBL1097442 ChEMBL	P0A031	—	363.3 Da LogP 2.35 TPSA 108.3	✓ Ro5	✓ Clean	`NC(=O)c1ccc2sc(COc3ccc(F)c(C(N)=O)c3F)nc2c1`
CHEMBL1097443 ChEMBL	P0A031	—	364.3 Da LogP 2.95 TPSA 102.5	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OCc2nc3cc(C(=O)O)ccc3s2)c1F`
CHEMBL1097767 ChEMBL	P0A031	—	335.3 Da LogP 2.83 TPSA 91.2	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OCc2nc3cc(N)ccc3s2)c1F`
CHEMBL1097768 ChEMBL	P0A031	—	363.4 Da LogP 3.32 TPSA 68.5	✓ Ro5	✓ Clean	`CN(C)c1ccc2sc(COc3ccc(F)c(C(N)=O)c3F)nc2c1`
CHEMBL1097796 ChEMBL	P0A031	—	284.3 Da LogP 2.41 TPSA 65.2	✓ Ro5	✓ Clean	`Cc1cnc(COc2ccc(F)c(C(N)=O)c2F)s1`
CHEMBL1097798 ChEMBL	P0A031	—	267.2 Da LogP 1.34 TPSA 70.1	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OCCn2cccn2)c1F`
CHEMBL3361105 ChEMBL	P0A031	—	355.7 Da LogP 2.94 TPSA 70.8	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OC[C@@H]2COc3ccc(Cl)cc3O2)c1F`
CHEMBL3909931 ChEMBL	P0A031	—	379.3 Da LogP 2.07 TPSA 97.1	✓ Ro5	✓ Clean	`COC(=O)c1ccc2c(c1)OC(COc1ccc(F)c(C(N)=O)c1F)CO2`
CHEMBL3941121 ChEMBL	P0A031	—	345.3 Da LogP 2.26 TPSA 70.8	✓ Ro5	✓ Clean	`C#Cc1ccc2c(c1)OC(COc1ccc(F)c(C(N)=O)c1F)CO2`
CHEMBL4282358 ChEMBL	P17865	—	386.4 Da LogP 4.60 TPSA 78.4	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(-c2cc(COc3ccc(F)c(C(N)=O)c3F)no2)…`
CHEMBL461450 ChEMBL	P0A031	—	299.4 Da LogP 4.19 TPSA 52.3	✓ Ro5	✓ Clean	`CCCCCCCCCOc1ccc(F)c(C(N)=O)c1F`
CHEMBL5084076 ChEMBL	A5Z1V5	—	379.3 Da LogP 2.00 TPSA 146.4	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OCCNc2ccc([N+](=O)[O-])c3nonc23…`
CHEMBL5092407 ChEMBL	A5Z1V5	—	421.4 Da LogP 3.17 TPSA 146.4	✓ Ro5	✓ Clean	`CCCC(CNc1ccc([N+](=O)[O-])c2nonc12)Oc1ccc(F)c(C…`
CHEMBL5402658 ChEMBL	P0A031	—	387.8 Da LogP 5.27 TPSA 52.3	1 viol.	✓ Clean	`Cc1cc(Cl)ccc1-c1cccc(COc2ccc(F)c(C(N)=O)c2F)c1`
G2P ChEMBL	A5Z1V5	—	521.2 Da LogP -2.22 TPSA 289.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`

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
ZINC3861633 ZINC	1.000	256.2 Da LogP 1.58 TPSA 94.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)c(O)cc(O)c21`
ZINC40878032 ZINC	1.000	355.8 Da LogP 3.30 TPSA 78.1	✓ Ro5	✓ Clean	`NC(=O)c1c(F)ccc(OCc2nc3cc(Cl)cnc3s2)c1F`
ZINC104869865 ZINC	0.864	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289 ZINC	0.864	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308 ZINC	0.864	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839 ZINC	0.864	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491 ZINC	0.864	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694 ZINC	0.864	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481 ZINC	0.864	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC12501413 ZINC	0.797	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC12958448 ZINC	0.797	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC1532555 ZINC	0.797	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC16546189 ZINC	0.797	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC2159505 ZINC	0.797	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3073318 ZINC	0.797	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869963 ZINC	0.797	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869965 ZINC	0.797	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC9334496 ZINC	0.797	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC12655867 ZINC	0.778	478.4 Da LogP 3.73 TPSA 149.2	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)c(-c3cc(O)c4c(c3O)C(=O)c…`
ZINC2168289 ZINC	0.741	270.3 Da LogP 2.77 TPSA 52.6	✓ Ro5	Alert	`COc1cccc(C(=O)C(=O)c2cccc(OC)c2)c1`
ZINC9315264 ZINC	0.735	270.3 Da LogP 2.05 TPSA 81.4	✓ Ro5	✓ Clean	`COc1cccc(C(=O)Nc2cccc(C(N)=O)c2)c1`
ZINC2574623 ZINC	0.714	242.3 Da LogP 2.93 TPSA 35.5	✓ Ro5	✓ Clean	`COc1cccc(C(=O)c2cccc(OC)c2)c1`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC4098664 ZINC	0.700	254.2 Da LogP 2.18 TPSA 74.6	✓ Ro5	Alert	`Cc1cc(O)c2c(c1O)C(=O)c1ccccc1C2=O`
ZINC4404481 ZINC	0.700	274.7 Da LogP 2.53 TPSA 74.6	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)c(Cl)cc(O)c21`
ZINC71774763 ZINC	0.691	432.3 Da LogP -2.23 TPSA 198.3	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@](=O)(O)N3CCOCC3…`
ZINC5699363 ZINC	0.680	304.2 Da LogP 0.70 TPSA 155.5	1 viol.	Alert	`O=C1c2c(O)cc(O)c(O)c2C(=O)c2c(O)cc(O)c(O)c21`
ZINC4743771 ZINC	0.672	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC4743772 ZINC	0.672	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC4743774 ZINC	0.672	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC4743775 ZINC	0.672	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC3873983 ZINC	0.667	255.2 Da LogP 1.46 TPSA 100.6	✓ Ro5	Alert	`Nc1c(O)cc(O)c2c1C(=O)c1ccccc1C2=O`
ZINC4411268 ZINC	0.667	288.2 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`O=C1c2c(O)ccc(O)c2C(=O)c2c(O)c(O)cc(O)c21`
ZINC465182 ZINC	0.667	227.3 Da LogP 2.46 TPSA 52.3	✓ Ro5	✓ Clean	`COc1ccc(-c2cccc(C(N)=O)c2)cc1`
ZINC12503703 ZINC	0.657	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC8215878 ZINC	0.657	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O…`
ZINC13327810 ZINC	0.656	270.2 Da LogP 1.37 TPSA 94.8	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)c(CO)cc(O)c21`
ZINC13481221 ZINC	0.656	284.2 Da LogP 1.57 TPSA 111.9	✓ Ro5	Alert	`O=C(O)c1cc(O)c2c(c1O)C(=O)c1ccccc1C2=O`
ZINC3875972 ZINC	0.656	320.3 Da LogP 1.12 TPSA 129.0	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)c(S(=O)(=O)O)cc(O)c21`
ZINC3847495 ZINC	0.654	240.2 Da LogP 1.87 TPSA 74.6	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)ccc(O)c21`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC100058967 ZINC	0.652	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@H]3O[C@H](CO[P@](=O)(O)OP(=O)…`
ZINC12504287 ZINC	0.652	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(…`
ZINC12504288 ZINC	0.652	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC31308647 ZINC	0.652	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(…`
ZINC38580950 ZINC	0.650	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@H](O…`
ZINC3869968 ZINC	0.650	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)…`
ZINC6585367 ZINC	0.650	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)…`

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.