KpKP13 Protein target profile

Phospho-N-acetylmuramoyl-pentapeptide- transferase

Accession: KP13_01908

Gene: mraY AHE46349.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GI63

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Length 360

Pocket druggability (P2Rank · AlphaFold DB model) 0.848

Direct ligand evidence 0 37 total records

Functional annotation 1 EC 10 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

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: No hit
Gut microbiome similarity: 6.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 98.056 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 91.95 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) 0.848

Structure A0A0H3GI63

Pocket Pocket 1

Druggability (FPocket) 0.685

Structure A0A0H3GI63

Pocket Pocket 2

ColabFold model

P2Rank 0.818 · Pocket 1

FPocket 0.857 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 320 / 4744 genomes with a hit

Prevalence 6.7%

Sequence

Primary amino-acid sequence viewer.

MLVWLAEHLVKYYSGFNVFSYLTFRAIVSLLTALFISLWMGPRMIARLQKLAFGQVVRNDGPESHFSKRGTPTMGGIMILTAITVSVLLWAYPSNPYVWCVLTVLIGYGIIGFVDDYRKVVRKDTKGLIARWKYFWMSVIALGVAFALYLAGKDTPATELVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNMNFANYLHIPYLRHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVETLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLATLKVR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

2.7.8.13

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0008963 Catalysis of the reaction: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine = Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + UMP.
GO:0016780 Catalysis of the transfer of a substituted phosphate group, other than diphosphate or nucleotidyl residues, from one compound (donor) to a another (acceptor).
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:0051992 Catalysis of the reaction: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP.
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:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
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.

46 records

Show feature table

Start	End	DB	Term	Name
358	360	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
234	256	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
285	289	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
61	356	CDD	cd06852	GT_MraY
61	356	InterPro	IPR003524	Phospho-N-acetylmuramoyl-pentapeptide transferase
1	19	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
68	80	Pfam	PF10555	Phospho-N-acetylmuramoyl-pentapeptide-transferase signature 1
68	80	InterPro	IPR018480	Phospho-N-acetylmuramoyl-pentapeptide transferase, conserved site
20	40	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
25	358	Hamap	MF_00038	Phospho-N-acetylmuramoyl-pentapeptide-transferase [mraY].
25	358	InterPro	IPR003524	Phospho-N-acetylmuramoyl-pentapeptide transferase
200	219	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
68	80	ProSitePatterns	PS01347	MraY family signature 1.
338	357	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
115	133	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
20	42	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
99	284	Pfam	PF00953	Glycosyl transferase family 4
99	284	InterPro	IPR000715	Glycosyl transferase, family 4
41	72	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
263	285	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
194	199	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
134	152	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
200	219	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
134	151	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
257	262	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
220	238	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
97	114	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
37	360	NCBIfam	TIGR00445	phospho-N-acetylmuramoyl-pentapeptide-transferase
37	360	InterPro	IPR003524	Phospho-N-acetylmuramoyl-pentapeptide transferase
312	337	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
289	311	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
23	358	PANTHER	PTHR22926	PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
23	358	InterPro	IPR000715	Glycosyl transferase, family 4
239	256	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
96	114	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
153	171	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
290	311	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
75	92	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
172	193	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
73	90	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
171	193	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
263	284	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
189	200	ProSitePatterns	PS01348	MraY family signature 2.
189	200	InterPro	IPR018480	Phospho-N-acetylmuramoyl-pentapeptide transferase, conserved site
91	95	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
338	357	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; 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

0.848

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Surrounding area

Pocket 2 P2Rank #2

0.168

Likely same site as FPocket 2 0.6 Å 13 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.14

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Surrounding area

Pocket 4 P2Rank #4

0.041

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Surrounding area

Pocket 5 P2Rank #5

0.037

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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 #2

0.685

Likely same site as P2Rank 2 0.6 Å 13 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #5

0.41

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Surrounding area

Pocket 3 FPocket #3

0.363

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Surrounding area

Residue sets

UniProt: Binding site:192-192

UniProt: Binding site:267-267

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.818

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Surrounding area

Pocket 2 P2Rank #2

0.301

Likely same site as FPocket 3 1.2 Å 13 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.122

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Surrounding area

Pocket 4 P2Rank #4

0.031

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Surrounding area

Pocket 5 P2Rank #5

0.026

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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_A0A0H3GI63	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01908	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.

37 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 37 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 35 direct and transferred ChEMBL records

Proposed compounds 0 similarity-based ZINC candidates

Best available ligand signal

NK4 PDB via homolog 798.0 Da · LogP 1.05 · TPSA 250.3 Open detail RCSB PDB

NKD PDB via homolog Detail RCSB PDB

CHEMBL4286766 ChEMBL via homolog · pchembl 10.80 (~0.0 nM) Detail ChEMBL

CHEMBL4284923 ChEMBL via homolog · pchembl 10.03 (~0.1 nM) Detail ChEMBL

CHEMBL4279378 ChEMBL via homolog · pchembl 9.49 (~0.3 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
NK4 RCSB PDB	6OYH	O66465	798.0 Da LogP 1.05 TPSA 250.3	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCC[C@H]1CN([C@H](C(=O)N([C@@H]1C…`
NKD RCSB PDB	6OZ6	O66465	856.9 Da LogP -1.83 TPSA 328.0	3 viol.	✓ Clean	`C[C@@H]([C@@H](C(=O)N/C=C\1/[C@H]([C@H]([C@@H](…`

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
CHEMBL4286766 ChEMBL	P0C1R8	10.80 ~0.0 nM	946.0 Da LogP -6.69 TPSA 432.6	3 viol.	✓ Clean	`CO[C@H]1[C@H](O[C@H]([C@H]2O[C@@H](n3ccc(=O)[nH…`
CHEMBL4284923 ChEMBL	P0C1R8	10.03 ~0.1 nM	988.0 Da LogP -6.51 TPSA 435.7	3 viol.	✓ Clean	`CO[C@H]1[C@H](O[C@H]([C@H]2O[C@@H](n3ccc(=O)[nH…`
CHEMBL4279378 ChEMBL	O66465	9.49 ~0.3 nM	1156.3 Da LogP -1.58 TPSA 438.7	3 viol.	✓ Clean	`CO[C@H]1[C@H](O[C@H]([C@H]2O[C@@H](n3ccc(=O)[nH…`
CHEMBL4475677 ChEMBL	P0C1R8	8.59 ~2.6 nM	784.0 Da LogP 0.71 TPSA 259.1	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCC[C@@H]1CN[C@@H]([C@H](O[C@@H]2…`
57M ChEMBL	Q03521	8.12 ~7.6 nM	916.0 Da LogP -6.52 TPSA 425.9	3 viol.	✓ Clean	`CC(C)C[C@@H](C(=O)NCCCN[C@@H]([C@@H]([C@@H]1[C@…`
CHEMBL5282738 ChEMBL	E2QF15	8.00 ~10.0 nM	649.7 Da LogP -3.07 TPSA 242.8	3 viol.	✓ Clean	`CO[C@H]1[C@@H](OC)[C@H](n2ccc(=O)[nH]c2=O)O[C@@…`
CHEMBL4283943 ChEMBL	P9WMW7	7.96 ~11.0 nM	930.0 Da LogP -5.66 TPSA 412.4	3 viol.	✓ Clean	`CO[C@H]1[C@H](O[C@H]([C@H]2O[C@@H](n3ccc(=O)[nH…`
CHEMBL5265940 ChEMBL	P0C1R8	7.77 ~17.0 nM	583.6 Da LogP -4.18 TPSA 253.8	3 viol.	✓ Clean	`CO[C@H]1[C@@H](O)[C@H](n2ccc(=O)[nH]c2=O)O[C@@H…`
CHEMBL95027 ChEMBL	P0A6W3	7.77 ~17.0 nM	583.6 Da LogP -4.18 TPSA 253.8	3 viol.	✓ Clean	`CO[C@H]1[C@@H](O)[C@H](n2ccc(=O)[nH]c2=O)O[C@@H…`
NKM ChEMBL	P0A6W3	7.75 ~17.8 nM	569.5 Da LogP -4.57 TPSA 253.8	3 viol.	✓ Clean	`CO[C@H]1[C@H]([C@@H](O[C@@H]1[C@H](C(=O)N)O[C@@…`
CHEMBL2048825 ChEMBL	P0C1R8	7.66 ~21.9 nM	711.7 Da LogP -1.68 TPSA 283.1	3 viol.	✓ Clean	`C[C@H](N)C(=O)N(C)[C@@H](C)[C@H](NC(=O)[C@H](C)…`
CHEMBL2048828 ChEMBL	P0C1R8	7.66 ~21.9 nM	876.9 Da LogP -2.67 TPSA 352.6	3 viol.	✓ Clean	`C[C@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)C…`
CHEMBL5272467 ChEMBL	Q03521	7.66 ~21.9 nM	726.7 Da LogP -2.74 TPSA 309.1	3 viol.	✓ Clean	`C[C@@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)…`
CHEMBL4473600 ChEMBL	P0C1R8	7.62 ~24.0 nM	711.9 Da LogP 0.66 TPSA 230.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)N[C@H]1CCN[C@H]([C@H](O[C@@…`
CHEMBL5277590 ChEMBL	P0C1R8	7.57 ~26.9 nM	473.4 Da LogP -4.18 TPSA 221.9	1 viol.	✓ Clean	`COC(=O)C1=C[C@@H](O)[C@@H](O)[C@H](O[C@@H](C(N)…`
CHEMBL2048826 ChEMBL	P0C1R8	7.38 ~41.7 nM	727.7 Da LogP -2.71 TPSA 303.3	3 viol.	✓ Clean	`C[C@H](N)C(=O)N(C)[C@@H](C)[C@H](NC(=O)[C@H](C)…`
CHEMBL5271984 ChEMBL	Q03521	7.38 ~41.7 nM	713.7 Da LogP -3.05 TPSA 312.1	3 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@@H](C)[C@H](NC(=O)[C@H](C)NC(…`
CHEMBL1780217 ChEMBL	Q03521	7.31 ~49.0 nM	916.0 Da LogP -6.31 TPSA 423.4	3 viol.	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@@H](NC(=O)N[C@H](C(=O)O)C…`
CHEMBL5278937 ChEMBL	E2QF15	7.24 ~57.5 nM	601.6 Da LogP -4.62 TPSA 253.8	3 viol.	✓ Clean	`CO[C@H]1[C@@H](O)[C@H](n2ccc(=O)[nH]c2=O)O[C@@H…`
CHEMBL2048830 ChEMBL	P0C1R8	7.19 ~64.6 nM	713.7 Da LogP -3.10 TPSA 303.3	3 viol.	✓ Clean	`C[C@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)C…`
CHEMBL1780218 ChEMBL	Q03521	6.61 ~245.5 nM	1070.3 Da LogP -1.88 TPSA 423.4	3 viol.	✓ Clean	`CCCCCCCCCCCCCCC[C@H](NC(=O)[C@@H](NC(=O)N[C@H](…`
9LH ChEMBL	P0C1R8	6.60 ~251.2 nM	830.9 Da LogP -2.48 TPSA 311.8	3 viol.	✓ Clean	`CC(C)CCCCCCCCC/C=C/C(=O)N[C@@H]1[C@H]([C@H]([C@…`
CHEMBL5279603 ChEMBL	P0C1R8	6.52 ~302.0 nM	490.5 Da LogP -3.42 TPSA 215.5	2 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(N)cc2)[C@H]2O[…`
CHEMBL5267618 ChEMBL	P0A6W3	6.48 ~331.1 nM	502.6 Da LogP -2.49 TPSA 201.5	3 viol.	✓ Clean	`CCCCCCCNCC(O[C@@H]1O[C@H](CN)[C@@H](O)[C@H]1O)[…`
CHEMBL5275061 ChEMBL	P0A6W3	6.48 ~331.1 nM	586.7 Da LogP -0.15 TPSA 201.5	3 viol.	✓ Clean	`CCCCCCCCCCCCCNCC(O[C@@H]1O[C@H](CN)[C@@H](O)[C@…`
CHEMBL5276993 ChEMBL	P0A6W3	6.48 ~331.1 nM	558.7 Da LogP -0.93 TPSA 201.5	3 viol.	✓ Clean	`CCCCCCCCCCCNCC(O[C@@H]1O[C@H](CN)[C@@H](O)[C@H]…`
CHEMBL5281271 ChEMBL	P0A6W3	6.48 ~331.1 nM	460.5 Da LogP -3.66 TPSA 201.5	2 viol.	✓ Clean	`CCCCNCC(O[C@@H]1O[C@H](CN)[C@@H](O)[C@H]1O)[C@H…`
CHEMBL5288850 ChEMBL	P0A6W3	6.48 ~331.1 nM	530.6 Da LogP -1.71 TPSA 201.5	3 viol.	✓ Clean	`CCCCCCCCCNCC(O[C@@H]1O[C@H](CN)[C@@H](O)[C@H]1O…`
CHEMBL5289885 ChEMBL	P0C1R8	6.23 ~588.8 nM	551.6 Da LogP -1.33 TPSA 189.5	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(-c3ccccc3)cc2)…`
CHEMBL2048831 ChEMBL	P0C1R8	6.19 ~645.7 nM	876.9 Da LogP -2.67 TPSA 352.6	3 viol.	✓ Clean	`C[C@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)C…`
CHEMBL5277496 ChEMBL	P0C1R8	6.19 ~645.7 nM	551.6 Da LogP -1.33 TPSA 189.5	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2cccc(-c3ccccc3)c2)…`
CHEMBL1780219 ChEMBL	Q03521	6.16 ~691.8 nM	1070.3 Da LogP -1.88 TPSA 423.4	3 viol.	✓ Clean	`CCCCCCCCCCCCCCC[C@@H](NC(=O)[C@@H](NC(=O)N[C@H]…`
CHEMBL5287014 ChEMBL	P0C1R8	6.05 ~891.3 nM	594.6 Da LogP -1.75 TPSA 218.6	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(C(=O)Nc3ccccc3…`
CHEMBL5268197 ChEMBL	P0C1R8	6.02 ~955.0 nM	630.6 Da LogP -2.20 TPSA 235.7	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2cccc(NS(=O)(=O)c3c…`
CHEMBL5291217 ChEMBL	P0C1R8	6.00 ~1.0 µM	630.6 Da LogP -2.20 TPSA 235.7	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(NS(=O)(=O)c3cc…`

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

No virtual-screening candidates for this protein.

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 A0A0H3GI63

Chemistry

ChEMBL CHEMBL4286766 ChEMBL CHEMBL4284923 ChEMBL CHEMBL4279378 ChEMBL CHEMBL4475677 ChEMBL 57M ChEMBL CHEMBL5282738 ChEMBL CHEMBL4283943 ChEMBL CHEMBL5265940 ChEMBL CHEMBL95027 ChEMBL NKM ChEMBL CHEMBL2048825 ChEMBL CHEMBL2048828 ChEMBL CHEMBL5272467 ChEMBL CHEMBL4473600 ChEMBL CHEMBL5277590 ChEMBL CHEMBL2048826 ChEMBL CHEMBL5271984 ChEMBL CHEMBL1780217 ChEMBL CHEMBL5278937 ChEMBL CHEMBL2048830 ChEMBL CHEMBL1780218 ChEMBL 9LH ChEMBL CHEMBL5279603 ChEMBL CHEMBL5267618 ChEMBL CHEMBL5275061 ChEMBL CHEMBL5276993 ChEMBL CHEMBL5281271 ChEMBL CHEMBL5288850 ChEMBL CHEMBL5289885 ChEMBL CHEMBL2048831 ChEMBL CHEMBL5277496 ChEMBL CHEMBL1780219 ChEMBL CHEMBL5287014 ChEMBL CHEMBL5268197 ChEMBL CHEMBL5291217