KpATCC43816 Protein target profile

undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase

Accession: VK055_3191

Gene: AIK81759.1 wecA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GPT7

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Length 367

Pocket druggability (P2Rank · AlphaFold DB model) 0.841

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 27 total records

Functional annotation 1 EC 13 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 91.5% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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: 2.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 73.066 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 91.06 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) 0.841

Structure A0A0H3GPT7

Pocket Pocket 1

Druggability (FPocket) 0.433

Structure A0A0H3GPT7

Pocket Pocket 32

ColabFold model

P2Rank 0.84 · Pocket 1

FPocket 0.872 · Pocket 18

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 133 / 4744 genomes with a hit

Prevalence 2.8%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction, no isoenzyme backup detected, more central than 91.5% of genes in this genome, no human homolog detected.

Relative network centrality 91.5% more central than 91.5% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MNLLTAITELISIFLFTTLFIFVARKVAKKIGLVDKPNYRKRHQGLIPLVGGISVYAGICFTFAIADYYIPHASLYLACAGVLVLVGALDDRFDISVKIRAVIQAAIAVIMMMAGNLHLSSLGFIFGSWELVLGPFGFFLTLFAVWAAINAFNMVDGIDGLLGGLSSVSFAATGIILWFDGQYSLAMWCFAMIAAILPYILLNLGALGRRYKVFMGDAGSTMIGFTIIWILLETTQGKTHPISPVTALWIIAIPLMDMVAIMYRRLRKGMSPFSPDRQHIHHLIMRAGFTSRQAFVLITLAAALLALVGVVAEYTRIVPEWVMLILFLVAFFLYGYCIKRAWKVARLVKRIRRRIRRHSGNNPKLTK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 13 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

2.7.8.33

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0036380 Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol.
GO:0009103 The chemical reactions and pathways resulting in the formation of lipopolysaccharides, any of a group of related, structurally complex components of the outer membrane of Gram-negative bacteria.
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:0030145 Binding to a manganese ion (Mn).
GO:0009276 The peptidoglycan layer of the Gram-negative cell envelope. In Gram-negative cells the peptidoglycan is relatively thin (1-2nm) and is linked to the outer membrane by lipoproteins. In Gram-negative cells the peptidoglycan is too thin to retain the primary stain in the Gram staining procedure and therefore cells appear red after Gram stain.
GO:0000287 Binding to a magnesium (Mg) ion.
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:0016757 Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
GO:0044038 The chemical reactions and pathways resulting in the formation of a macromolecule destined to form part of a cell wall.
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:0009246 The chemical reactions and pathways resulting in the formation of the enterobacterial common antigen, an acidic polysaccharide containing N-acetyl-D-glucosamine, N-acetyl-D-mannosaminouronic acid, and 4-acetamido-4,6-dideoxy-D-galactose. A major component of the cell wall outer membrane of Gram-negative bacteria.
GO:0009243 The chemical reactions and pathways resulting in the formation of the O side chain of a lipopolysaccharide, which determines the antigenic specificity of the organism. It is made up of about 50 repeating units of a branched tetrasaccharide.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
180	184	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
132	149	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
45	66	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
161	179	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
101	126	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
233	243	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
185	202	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
4	23	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
150	160	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
184	206	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
127	131	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
214	232	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
76	232	Pfam	PF00953	Glycosyl transferase family 4
76	232	InterPro	IPR000715	Glycosyl transferase, family 4
90	100	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
321	342	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
3	312	PANTHER	PTHR22926	PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
3	312	InterPro	IPR000715	Glycosyl transferase, family 4
203	213	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
70	89	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
8	350	NCBIfam	TIGR02380	UDP-N-acetylglucosamine--undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
8	350	InterPro	IPR012750	Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase
40	289	CDD	cd06853	GT_WecA_like
264	293	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
67	71	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
321	338	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
244	263	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
72	89	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
44	66	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
9	353	Hamap	MF_02030	Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase [wecA].
9	353	InterPro	IPR012750	Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase
294	315	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
105	127	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
160	179	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
242	261	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	5	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
25	44	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
6	24	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
343	367	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
294	311	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
131	153	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
213	232	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
316	320	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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

0.841

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Surrounding area

Pocket 2 P2Rank #2

0.74

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Surrounding area

Pocket 3 P2Rank #3

0.468

Likely same site as FPocket 13 1.9 Å 12 shared residues 92% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.276

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Surrounding area

Pocket 5 P2Rank #5

0.045

Likely same site as FPocket 32 2.3 Å 8 shared residues 89% 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 #32

0.433 Unusual size

Likely same site as P2Rank 5 2.3 Å 8 shared residues 89% of smaller site

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Surrounding area

Pocket 2 FPocket #13

0.399

Likely same site as P2Rank 3 1.9 Å 12 shared residues 92% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:153-153

UniProt: Binding site:217-217

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.84

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Surrounding area

Pocket 2 P2Rank #2

0.716

Likely same site as FPocket 18 2.4 Å 15 shared residues 83% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.325

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Surrounding area

Pocket 4 P2Rank #4

0.124

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Surrounding area

Pocket 5 P2Rank #5

0.066

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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 #18

0.872

Likely same site as P2Rank 2 2.4 Å 15 shared residues 83% of smaller site

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Surrounding area

Pocket 2 FPocket #29

0.736 Unusual size

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Surrounding area

Pocket 3 FPocket #2

0.229

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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_A0A0H3GPT7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3191	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.

27 records

Chemistry signal

Bioactivity evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 26 records from similar proteins

Structural ligands 0 0 loaded crystals

Measured bioactivity 26 direct and transferred ChEMBL records

Proposed compounds 1 similarity-based ZINC candidates

Best available ligand signal

CHEMBL4286766 ChEMBL via homolog pchembl 10.80 (~0.0 nM) 946.0 Da · LogP -6.69 · TPSA 432.6 Open detail ChEMBL

CHEMBL4279378 ChEMBL via homolog · pchembl 10.66 (~0.0 nM) Detail ChEMBL

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

CHEMBL4475677 ChEMBL via homolog · pchembl 8.59 (~2.6 nM) Detail ChEMBL

57M ChEMBL via homolog · pchembl 8.12 (~7.6 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.

No PDB ligands found through similar proteins.

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…`
CHEMBL4279378 ChEMBL	P0C1R8	10.66 ~0.0 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…`
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…`
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@…`
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…`
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…`
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[…`
NKM ChEMBL	P0C1R8	6.48 ~331.1 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@@…`
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).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC34752870 ZINC	0.500	257.2 Da LogP -2.23 TPSA 119.6	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](O)[C@@H](CN)O[C@H]1n1ccc(=O)[nH]…`

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.

undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase

Strong target candidate with converging metabolic, structural and chemical evidence.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways