KpKP13 Protein target profile

Rod shape-determining protein mreB

Accession: KP13_02966

Gene: mreB AHE42423.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GWB3

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Length 340

Pocket druggability (P2Rank · AlphaFold DB model) 0.966

Direct ligand evidence 0 62 total records

Functional annotation 0 EC 4 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.97, FPocket 0.90). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.90. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.97. Review the complete evidence below

Risks to review

Evidence gaps

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

Terms and data sources used on 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 Target 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.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 29.63 Lower values reduce human off-target concern.
Human E-value: 9.89e-08
Gut microbiome similarity: 56.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 99.412 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 92.44 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.966

Structure A0A0H3GWB3

Pocket Pocket 1

Druggability (FPocket) 0.897

Structure A0A0H3GWB3

Pocket Pocket 1

ColabFold model

P2Rank 0.959 · Pocket 1

FPocket 0.994 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 2679 / 4744 genomes with a hit

Prevalence 56.5%

Sequence

Primary amino-acid sequence viewer.

MFSNDLSIDLGTANTLIYVKGQGIVLNEPSVVAIRQDRAGSPKSVAAVGHEAKQMLGRTPGNIAAIRPMKDGVIADFFVTEKMLQHFIKQVHSNSFMRPSPRVLVCVPVGATQVERRAIRESAQGAGAREVFLIEEPMAAAIGAGLPVSEATGSMVVDIGGGTTEVAVISLNGVVYSSSVRIGGDRFDEAVINYVRRNYGSLIGEATAERIKHEIGSAYPGDEVREIEVRGRNLAEGVPRGFTLNSNEILEALQEPLTGIVSAVMVALEQCPPELASDISERGMVLTGGGALLRNLDRLLMEETGIPVVVAEDPLTCVARGGGKALEMIDMHGGDLFSEE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0000902 The developmental process in which the size or shape of a cell is generated and organized.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0008360 Any process that modulates the surface configuration of a cell.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
2	145	SUPERFAMILY	SSF53067	Actin-like ATPase domain
2	145	InterPro	IPR043129	ATPase, nucleotide binding domain
4	331	Pfam	PF06723	MreB/Mbl protein
238	314	FunFam	G3DSA:3.30.420.40:FF:000019	Rod shape-determining protein MreB
146	333	SUPERFAMILY	SSF53067	Actin-like ATPase domain
146	333	InterPro	IPR043129	ATPase, nucleotide binding domain
155	237	Gene3D	G3DSA:3.30.420.40	-
2	332	NCBIfam	TIGR00904	MreB/Mrl family cell shape determining protein
2	332	InterPro	IPR004753	Cell shape determining protein MreB
155	237	FunFam	G3DSA:3.30.420.40:FF:000016	Rod shape-determining protein mreB
3	337	Hamap	MF_02207	Cell shape-determining protein MreB [mreB].
3	337	InterPro	IPR004753	Cell shape determining protein MreB
238	314	Gene3D	G3DSA:3.30.420.40	-
2	335	PANTHER	PTHR42749	CELL SHAPE-DETERMINING PROTEIN MREB
1	154	Gene3D	G3DSA:3.30.420.40	-
1	154	FunFam	G3DSA:3.30.420.40:FF:000014	Rod shape-determining protein MreB
297	323	PRINTS	PR01652	Bacterial cell shape determinant MreB/Mbl protein signature
297	323	InterPro	IPR004753	Cell shape determining protein MreB
45	63	PRINTS	PR01652	Bacterial cell shape determinant MreB/Mbl protein signature
45	63	InterPro	IPR004753	Cell shape determining protein MreB
184	204	PRINTS	PR01652	Bacterial cell shape determinant MreB/Mbl protein signature
184	204	InterPro	IPR004753	Cell shape determining protein MreB
65	88	PRINTS	PR01652	Bacterial cell shape determinant MreB/Mbl protein signature
65	88	InterPro	IPR004753	Cell shape determining protein MreB
129	148	PRINTS	PR01652	Bacterial cell shape determinant MreB/Mbl protein signature
129	148	InterPro	IPR004753	Cell shape determining protein MreB
6	330	CDD	cd10225	MreB_like
6	330	InterPro	IPR004753	Cell shape determining protein MreB

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.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

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

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.966

Likely same site as FPocket 1 3.0 Å 30 shared residues 94% of smaller site

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #1

0.897 Unusual size

Likely same site as P2Rank 1 3.0 Å 30 shared residues 94% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:168-170

UniProt: Binding site:19-21

UniProt: Binding site:216-219

UniProt: Binding site:296-299

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #1

0.994

Likely same site as P2Rank 1 2.3 Å 28 shared residues 88% of smaller site

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Surrounding area

Pocket 2 FPocket #16

0.26

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

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
AlphaFold DB AF_A0A0H3GWB3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02966	ColabFold	—	—	full sequence	—	Loaded

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.

62 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 12 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 10 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ANP PDB via homolog 506.2 Da · LogP -2.06 · TPSA 281.9 Open detail RCSB PDB

NO7 PDB via homolog Detail RCSB PDB

DWT ChEMBL via homolog · pchembl 7.52 (~30.2 nM) Detail ChEMBL

DXH ChEMBL via homolog · pchembl 7.51 (~30.9 nM) Detail ChEMBL

EAM ChEMBL via homolog · pchembl 7.07 (~85.1 nM) Detail ChEMBL

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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
ANP RCSB PDB	4CZM	A0A0H3C7V4	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)…`
NO7 RCSB PDB	6P2U	P38646	465.3 Da LogP -1.28 TPSA 218.6	2 viol.	✓ Clean	`C#CCNc1c2c(ncn1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=…`

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
DWT ChEMBL	P38646	7.52 ~30.2 nM	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
DXH ChEMBL	P38646	7.51 ~30.9 nM	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cnn(c3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
EAM ChEMBL	P38646	7.07 ~85.1 nM	423.9 Da LogP 3.66 TPSA 81.4	✓ Ro5	✓ Clean	`CCNC(=O)C[C@H]1c2nnc(n2-c3ccc(cc3C(=N1)c4ccc(cc…`
CHEMBL4649247 ChEMBL	P38646	6.52 ~302.0 nM	396.4 Da LogP 4.31 TPSA 104.6	✓ Ro5	✓ Clean	`CN1c2ccc(NC(=O)Nc3ccc([N+](=O)[O-])cc3)cc2C(C)(…`
CHEMBL4646130 ChEMBL	P38646	6.30 ~501.2 nM	398.5 Da LogP 5.30 TPSA 70.4	1 viol.	✓ Clean	`CN1c2ccc(NC(=S)Nc3ccc([N+](=O)[O-])cc3)cc2C(C)(…`
CHEMBL7075 ChEMBL	P38646	6.22 ~602.6 nM	401.6 Da LogP 5.96 TPSA 67.2	1 viol.	✓ Clean	`CC1(C)CC(C)(C)c2cc(NC(=S)Nc3ccc([N+](=O)[O-])cc…`
CHEMBL4639280 ChEMBL	P38646	6.16 ~691.8 nM	496.3 Da LogP 1.49 TPSA 84.3	✓ Ro5	Alert	`CC1(C)CC[N+](C)(C)c2ccc(NC(=O)Nc3ccc([N+](=O)[O…`
CHEMBL4648396 ChEMBL	P38646	6.16 ~691.8 nM	421.5 Da LogP 5.22 TPSA 64.6	1 viol.	✓ Clean	`CN1c2ccc(NC(=O)Nc3ccc(C(F)(F)F)cc3)cc2C(C)(C)C(…`
CHEMBL4872862 ChEMBL	P38646	—	447.6 Da LogP 4.62 TPSA 65.4	✓ Ro5	✓ Clean	`N#CC1=C(NCCN2CCOCC2)c2ccc(SC3CCCCC3)c3cccc(c23)…`
CHEMBL5424525 ChEMBL	P38646	—	309.4 Da LogP 2.60 TPSA 71.1	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)c1cccs1)C(=O)Nc1nccs1`

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
ZINC58655571 ZINC	1.000	423.9 Da LogP 3.66 TPSA 81.4	✓ Ro5	✓ Clean	`CCNC(=O)C[C@@H]1N=C(c2ccc(Cl)cc2)c2cc(OC)ccc2-n…`
ZINC72190293 ZINC	1.000	423.9 Da LogP 3.66 TPSA 81.4	✓ Ro5	✓ Clean	`CCNC(=O)C[C@H]1N=C(c2ccc(Cl)cc2)c2cc(OC)ccc2-n2…`
ZINC7276870 ZINC	1.000	309.4 Da LogP 2.60 TPSA 71.1	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)c1cccs1)C(=O)Nc1nccs1`
ZINC7276877 ZINC	1.000	309.4 Da LogP 2.60 TPSA 71.1	✓ Ro5	✓ Clean	`CC(C)[C@@H](NC(=O)c1cccs1)C(=O)Nc1nccs1`
ZINC198754825 ZINC	0.823	410.9 Da LogP 3.69 TPSA 78.6	✓ Ro5	✓ Clean	`COC(=O)C[C@H]1N=C(c2ccc(Cl)cc2)c2cc(OC)ccc2-n2c…`
ZINC96284849 ZINC	0.823	410.9 Da LogP 3.69 TPSA 78.6	✓ Ro5	✓ Clean	`COC(=O)C[C@@H]1N=C(c2ccc(Cl)cc2)c2cc(OC)ccc2-n2…`
ZINC12360002 ZINC	0.810	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 ZINC	0.810	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 ZINC	0.810	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 ZINC	0.810	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 ZINC	0.810	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 ZINC	0.810	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 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.810	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 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.810	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 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC144944720 ZINC	0.806	396.8 Da LogP 3.60 TPSA 89.6	✓ Ro5	✓ Clean	`COc1ccc2c(c1)C(c1ccc(Cl)cc1)=N[C@H](CC(=O)O)c1n…`
ZINC96284850 ZINC	0.806	396.8 Da LogP 3.60 TPSA 89.6	✓ Ro5	✓ Clean	`COc1ccc2c(c1)C(c1ccc(Cl)cc1)=N[C@@H](CC(=O)O)c1…`
ZINC13518964 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.741	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 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.741	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 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.741	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 ZINC	0.741	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 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC64859622 ZINC	0.731	409.9 Da LogP 3.35 TPSA 81.4	✓ Ro5	✓ Clean	`CCNC(=O)C[C@@H]1N=C(c2ccc(Cl)cc2)c2cc(OC)ccc2-n…`
ZINC4096224 ZINC	0.729	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850 ZINC	0.726	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 ZINC	0.726	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 ZINC	0.726	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 ZINC	0.726	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 ZINC	0.712	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 ZINC	0.712	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 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423 ZINC	0.703	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC12594026 ZINC	0.702	303.4 Da LogP 2.54 TPSA 71.1	✓ Ro5	✓ Clean	`CC(C)[C@@H](NC(=O)c1cccs1)C(=O)Nc1ccncc1`
ZINC12594030 ZINC	0.702	303.4 Da LogP 2.54 TPSA 71.1	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)c1cccs1)C(=O)Nc1ccncc1`
ZINC10624454 ZINC	0.700	323.4 Da LogP 2.91 TPSA 71.1	✓ Ro5	✓ Clean	`Cc1cnc(NC(=O)[C@H](NC(=O)c2cccs2)C(C)C)s1`
ZINC10624462 ZINC	0.700	323.4 Da LogP 2.91 TPSA 71.1	✓ Ro5	✓ Clean	`Cc1cnc(NC(=O)[C@@H](NC(=O)c2cccs2)C(C)C)s1`
ZINC3873852 ZINC	0.694	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 ZINC	0.694	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 ZINC	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=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.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GWB3

Chemistry

ChEMBL DWT ChEMBL DXH ChEMBL EAM ChEMBL CHEMBL4649247 ChEMBL CHEMBL4646130 ChEMBL CHEMBL7075 ChEMBL CHEMBL4639280 ChEMBL CHEMBL4648396 ChEMBL CHEMBL4872862 ChEMBL CHEMBL5424525