Protein target profile

KP13_31766

cell division protein FtsY

Genome: KpKP13 Gene: ftsY AHE42249.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GYJ7

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Length 507

Pocket druggability 0.076

Direct ligand evidence 0 59 total records

Functional annotation 1 EC 8 GO

Target summary

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

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing 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 (%): 34.975 Lower values reduce human off-target concern.
Human E-value: 1.48e-31
Gut microbiome similarity: 1.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 77.351 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 72.45 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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 0.076

Structure A0A0H3GYJ7

Pocket Pocket 32

P2Rank 0.129

Structure A0A0H3GYJ7

Pocket Pocket 1

ColabFold model

FPocket 0.284 · Pocket 2

P2Rank 0.173 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 60 / 4744 genomes with a hit

Prevalence 1.3%

Cross-references

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

Sequence

UniProt A0A0H3GYJ7

Sequence

Primary amino-acid sequence viewer.

MAKEKKRGFFSWLGFGQKEQAQETETEQKVEEQQAVAEEIPAVETPAEPSAPKADPEAFAEDVVEVTETVVESEKAHLAEPASAQEEEWVETPALTEETPVVEPEPAVSEPPEQPAVVEPLAEEVIAEPVVAEAVAEQTVEGIVVQPQETEAPEEDAPLSDEELEAQALAAEAAEEAAVVVPAPEDEAPLEALAQEQEKPTKEGFFARLKRSLLKTKQNLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITNLTEGASRKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKARHVDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVDAPHEVMLTIDASTGQNAISQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFNAGDFIEALFARED

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

3.6.5.4

Gene Ontology (GO)

GO:0006614 The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.
GO:0005525 Binding to GTP, guanosine triphosphate.
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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
GO:0005047 Binding to a signal recognition particle.
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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

35 records

Show feature table

Start	End	DB	Term	Name
193	293	Gene3D	G3DSA:1.20.120.140	-
193	293	InterPro	IPR042101	Signal recognition particle SRP54, N-terminal domain superfamily
232	503	NCBIfam	TIGR00064	signal recognition particle-docking protein FtsY
232	503	InterPro	IPR004390	Signal-recognition particle receptor FtsY
8	16	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	121	MobiDBLite	mobidb-lite	consensus disorder prediction
304	502	CDD	cd17874	FtsY
220	285	Pfam	PF02881	SRP54-type protein, helical bundle domain
220	285	InterPro	IPR013822	Signal recognition particle SRP54, helical bundle
1	7	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
232	504	Hamap	MF_00920	Signal recognition particle receptor FtsY [ftsY].
232	504	InterPro	IPR004390	Signal-recognition particle receptor FtsY
302	493	SMART	SM00382	AAA_5
302	493	InterPro	IPR003593	AAA+ ATPase domain
22	507	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
303	503	Pfam	PF00448	SRP54-type protein, GTPase domain
303	503	InterPro	IPR000897	Signal recognition particle, SRP54 subunit, GTPase domain
17	21	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
303	504	SMART	SM00962	SRP54_3
303	504	InterPro	IPR000897	Signal recognition particle, SRP54 subunit, GTPase domain
296	504	FunFam	G3DSA:3.40.50.300:FF:000053	Signal recognition particle receptor FtsY
295	507	Gene3D	G3DSA:3.40.50.300	-
295	507	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
1	21	Phobius	SIGNAL_PEPTIDE	Signal peptide region
199	293	FunFam	G3DSA:1.20.120.140:FF:000002	Signal recognition particle receptor FtsY
204	283	SUPERFAMILY	SSF47364	Domain of the SRP/SRP receptor G-proteins
204	283	InterPro	IPR036225	SRP/SRP receptor, N-terminal
209	289	SMART	SM00963	SRP54_N_2
209	289	InterPro	IPR013822	Signal recognition particle SRP54, helical bundle
477	490	ProSitePatterns	PS00300	SRP54-type proteins GTP-binding domain signature.
477	490	InterPro	IPR000897	Signal recognition particle, SRP54 subunit, GTPase domain
6	503	PANTHER	PTHR43134	SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA
296	503	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
296	503	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
68	84	MobiDBLite	mobidb-lite	consensus disorder prediction

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

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.129

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Surrounding area

Site 2 P2Rank #2

0.118

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Surrounding area

Site 3 P2Rank #3

0.075

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Surrounding area

Site 4 P2Rank #4

0.001

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:310-317

UniProt: Binding site:392-396

UniProt: Binding site:456-459

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_A0A0H3GYJ7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_31766	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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0O2 PDB via homolog 683.1 Da · LogP -2.10 · TPSA 392.2 Open detail RCSB PDB

4ME PDB via homolog Detail RCSB PDB

ALF PDB via homolog Detail RCSB PDB

F9Y PDB via homolog Detail RCSB PDB

GCP PDB via homolog Detail RCSB PDB

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
0O2 RCSB PDB	7O9H	P10121	683.1 Da LogP -2.10 TPSA 392.2	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…`
4ME RCSB PDB	6CVD	P10121	175.2 Da LogP 1.95 TPSA 42.1	✓ Ro5	✓ Clean	`COC(=O)c1cccc2c1cc[nH]2`
ALF RCSB PDB	4C7O	P10121	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
F9Y RCSB PDB	6CS8	P10121	142.2 Da LogP 2.04 TPSA 39.6	✓ Ro5	✓ Clean	`c1cc(cc2c1cc[nH]2)C#N`
GCP RCSB PDB	5L3R	O80842	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…`
GNP RCSB PDB	5NIY	P10121	522.2 Da LogP -2.76 TPSA 301.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GXY RCSB PDB	6DLX	P10121	232.1 Da LogP 2.05 TPSA 44.5	✓ Ro5	✓ Clean	`COc1cc(c(cc1Br)OC)N`
MLI RCSB PDB	2OG2	O80842	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
NH4 RCSB PDB	6CVD	P10121	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`

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).

No ChEMBL hits found through similar proteins.

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
ZINC9372393 ZINC	1.000	232.1 Da LogP 2.05 TPSA 44.5	✓ Ro5	✓ Clean	`COc1cc(Br)c(OC)cc1N`
ZINC34541308 ZINC	0.850	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)(…`
ZINC104869865 ZINC	0.836	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	0.836	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	0.836	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	0.836	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	0.836	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	0.836	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)(…`
ZINC36181635 ZINC	0.826	232.1 Da LogP 2.05 TPSA 44.5	✓ Ro5	✓ Clean	`COc1cc(OC)c(Br)cc1N`
ZINC39590917 ZINC	0.783	217.1 Da LogP 1.62 TPSA 61.3	✓ Ro5	✓ Clean	`COc1cc(N)c(N)cc1Br`
ZINC494861 ZINC	0.783	280.9 Da LogP 2.80 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(Br)c(Br)cc1N`
ZINC12501413 ZINC	0.770	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	0.770	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	0.770	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	0.770	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	0.770	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	0.770	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	0.770	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	0.770	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	0.770	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)[…`
ZINC72204055 ZINC	0.750	280.9 Da LogP 2.80 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(Br)c(N)cc1Br`
ZINC8737772 ZINC	0.750	280.9 Da LogP 2.80 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(N)c(Br)cc1Br`
ZINC16678131 ZINC	0.720	216.1 Da LogP 2.35 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(N)c(C)cc1Br`
ZINC4707252 ZINC	0.720	402.1 Da LogP 4.06 TPSA 70.5	✓ Ro5	✓ Clean	`COc1cc(-c2cc(OC)c(N)cc2Br)c(Br)cc1N`
ZINC57059 ZINC	0.714	296.0 Da LogP 3.23 TPSA 18.5	✓ Ro5	✓ Clean	`COc1cc(Br)c(OC)cc1Br`
ZINC1685331 ZINC	0.708	232.1 Da LogP 2.05 TPSA 44.5	✓ Ro5	✓ Clean	`COc1cc(N)c(Br)cc1OC`
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`
ZINC40571453 ZINC	0.692	216.1 Da LogP 2.35 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(Br)c(C)cc1N`
ZINC33358958 ZINC	0.686	203.2 Da LogP 1.31 TPSA 59.2	✓ Ro5	✓ Clean	`COC(=O)c1cccc2c(=O)[nH]ccc12`
ZINC71774763 ZINC	0.671	432.3 Da LogP -2.23 TPSA 198.3	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@](=O)(O)N3CCOCC3…`
ZINC14982814 ZINC	0.667	233.2 Da LogP 1.74 TPSA 68.4	✓ Ro5	✓ Clean	`COC(=O)c1cc(C(=O)OC)c2cc[nH]c2c1`
ZINC149859436 ZINC	0.667	327.9 Da LogP 2.64 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(N)c(I)cc1Br`
ZINC15444513 ZINC	0.667	236.5 Da LogP 2.69 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(Br)c(Cl)cc1N`
ZINC20283497 ZINC	0.667	304.3 Da LogP 2.55 TPSA 89.0	✓ Ro5	✓ Clean	`COc1cc(-c2cc(OC)c(N)cc2OC)c(OC)cc1N`
ZINC34363585 ZINC	0.667	236.5 Da LogP 2.69 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(N)c(Cl)cc1Br`
ZINC39619094 ZINC	0.667	220.0 Da LogP 2.18 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(N)c(F)cc1Br`
ZINC77032296 ZINC	0.667	220.0 Da LogP 2.18 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(Br)c(F)cc1N`
ZINC97447173 ZINC	0.667	218.0 Da LogP 1.75 TPSA 55.5	✓ Ro5	✓ Clean	`COc1cc(N)c(O)cc1Br`
ZINC97447174 ZINC	0.667	218.0 Da LogP 1.75 TPSA 55.5	✓ Ro5	✓ Clean	`COc1cc(Br)c(O)cc1N`
ZINC83428754 ZINC	0.654	216.1 Da LogP 2.35 TPSA 35.2	✓ Ro5	✓ Clean	`COc1cc(C)c(N)cc1Br`
ZINC163122 ZINC	0.652	247.1 Da LogP 2.47 TPSA 27.7	✓ Ro5	✓ Clean	`COc1cc(OC)c(OC)cc1Br`
ZINC1721293 ZINC	0.652	344.8 Da LogP 3.98 TPSA 9.2	✓ Ro5	✓ Clean	`COc1cc(Br)c(Br)cc1Br`
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`
ZINC4743771 ZINC	0.652	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	0.652	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	0.652	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	0.652	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…`
ZINC238405705 ZINC	0.649	203.2 Da LogP 1.31 TPSA 59.2	✓ Ro5	✓ Clean	`COC(=O)c1cccc2[nH]ccc(=O)c12`

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.

KP13_31766

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

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence