KpATCC43816 Protein target profile

nucleotide sugar dehydrogenase family protein

Accession: VK055_3188

Gene: AIK81756.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GLK6

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Length 420

Pocket druggability (P2Rank · AlphaFold DB model) 0.773

Direct ligand evidence 0 54 total records

Functional annotation 1 EC 6 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.

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.77. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 4 structural and 0 bioactivity records.

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: Hit
Human identity (%): 31.818 Lower values reduce human off-target concern.
Human E-value: 8.25e-06
Gut microbiome similarity: 4.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 31.776 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 96.26 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) 0.773

Structure A0A0H3GLK6

Pocket Pocket 1

Druggability (FPocket) 0.618

Structure A0A0H3GLK6

Pocket Pocket 2

ColabFold model

P2Rank 0.782 · Pocket 1

FPocket 0.83 · Pocket 13

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 227 / 4744 genomes with a hit

Prevalence 4.8%

Metabolic context

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

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSFSTISVIGLGYIGLPTAAAFASRQKRVVGVDVNQHAVETINRGEIHIVEPDLASVVKTAVEQGYLSATTTPVEADAYLIAVPTPFKDRHEPDMVFVESAAKSIAPTLKKGSLVILESTSPVGSTEQMAEWLAEMRPDLSFPQQVGEAADVNIAYCPERVLPGQVMVELIKNDRVIGGMSPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINVWELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDHKPEWVIEQVKAQVADCLNATNKRASELTIACFGLAFKPNIDDLRESPAMEIAAQIARWHSGTTQVVEPNIHALPKKLDGLCTLAPLEAALASADVLVMLVDHNQFKAVSGDSVTQAFIVDTKGVWR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.1.1.336

Gene Ontology (GO)

GO:0000271 The chemical reactions and pathways resulting in the formation of a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0089714 Catalysis of the reaction: UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O = UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+.
GO:0016628 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces NAD or NADP.
GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

34 records

Show feature table

Start	End	DB	Term	Name
238	420	Gene3D	G3DSA:3.40.50.720	-
1	202	FunFam	G3DSA:3.40.50.720:FF:000139	UDP-N-acetyl-D-mannosamine dehydrogenase
206	299	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
206	299	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
24	420	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	23	Phobius	SIGNAL_PEPTIDE	Signal peptide region
5	416	NCBIfam	TIGR03026	nucleotide sugar dehydrogenase
5	416	InterPro	IPR017476	UDP-glucose/GDP-mannose dehydrogenase
311	419	SUPERFAMILY	SSF52413	UDP-glucose/GDP-mannose dehydrogenase C-terminal domain
311	419	InterPro	IPR036220	UDP-glucose/GDP-mannose dehydrogenase, C-terminal domain superfamily
324	419	Pfam	PF03720	UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain
324	419	InterPro	IPR014027	UDP-glucose/GDP-mannose dehydrogenase, C-terminal
4	419	PIRSF	PIRSF000124	UDPglc_GDPman_dh
4	419	InterPro	IPR017476	UDP-glucose/GDP-mannose dehydrogenase
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
206	235	Gene3D	G3DSA:1.20.5.100	-
1	420	Hamap	MF_02029	UDP-N-acetyl-D-mannosamine dehydrogenase [wecC].
1	420	InterPro	IPR032891	UDP-N-acetyl-D-mannosamine dehydrogenase WecC
5	189	Pfam	PF03721	UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain
5	189	InterPro	IPR001732	UDP-glucose/GDP-mannose dehydrogenase, N-terminal
3	419	PANTHER	PTHR43491	UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE
3	419	InterPro	IPR028359	UDP-N-acetyl-D-mannosamine/glucosamine dehydrogenase
5	16	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
324	420	SMART	SM00984	UDPG_MGDP_dh_C_a_2_a
324	420	InterPro	IPR014027	UDP-glucose/GDP-mannose dehydrogenase, C-terminal
2	202	Gene3D	G3DSA:3.40.50.720	-
206	293	Pfam	PF00984	UDP-glucose/GDP-mannose dehydrogenase family, central domain
206	293	InterPro	IPR014026	UDP-glucose/GDP-mannose dehydrogenase, dimerisation
17	23	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
238	420	FunFam	G3DSA:3.40.50.720:FF:000235	UDP-N-acetyl-D-mannosamine dehydrogenase
1	420	PIRSF	PIRSF500136	UDP_ManNAc_DH
1	420	InterPro	IPR028359	UDP-N-acetyl-D-mannosamine/glucosamine dehydrogenase
5	198	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
5	198	InterPro	IPR036291	NAD(P)-binding domain superfamily

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

0.773

Likely same site as FPocket 11 0.2 Å 25 shared residues 89% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.663

Likely same site as FPocket 2 5.3 Å 17 shared residues 89% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.274

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Surrounding area

Pocket 4 P2Rank #4

0.235

Likely same site as FPocket 2 6.2 Å 16 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.126

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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

0.618 Unusual size

Likely same site as P2Rank 2 5.3 Å 17 shared residues 89% of smaller site

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Surrounding area

Pocket 2 FPocket #11

0.557 Unusual size

Likely same site as P2Rank 1 0.2 Å 25 shared residues 89% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:212-212 Proton donor/acceptor

UniProt: Active site:266-266 Nucleophile

UniProt: Binding site:126-126 in chain A

UniProt: Binding site:13-13 in chain A

UniProt: Binding site:14-14 in chain A

UniProt: Binding site:160-160 in chain A

UniProt: Binding site:161-161 in chain A

UniProt: Binding site:212-212 in chain A

UniProt: Binding site:216-216 in chain A

UniProt: Binding site:219-219 in chain A

UniProt: Binding site:250-250 in chain B

UniProt: Binding site:252-252 in chain B

UniProt: Binding site:263-263 in chain A

UniProt: Binding site:33-33 in chain A

UniProt: Binding site:330-330 in chain A

UniProt: Binding site:331-331 in chain A

UniProt: Binding site:338-338 in chain B

UniProt: Binding site:416-416 in chain A

UniProt: Binding site:85-85 in chain A

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.782

Likely same site as FPocket 8 0.9 Å 26 shared residues 93% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.716

Likely same site as FPocket 13 1.5 Å 19 shared residues 86% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.241

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Surrounding area

Pocket 4 P2Rank #4

0.169

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Surrounding area

Pocket 5 P2Rank #5

0.112

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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 #13

0.83

Likely same site as P2Rank 2 1.5 Å 19 shared residues 86% of smaller site

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Surrounding area

Pocket 2 FPocket #8

0.503 Unusual size

Likely same site as P2Rank 1 0.9 Å 26 shared residues 93% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:212-212 Proton donor/acceptor

UniProt: Active site:266-266 Nucleophile

UniProt: Binding site:126-126 in chain A

UniProt: Binding site:13-13 in chain A

UniProt: Binding site:14-14 in chain A

UniProt: Binding site:160-160 in chain A

UniProt: Binding site:161-161 in chain A

UniProt: Binding site:212-212 in chain A

UniProt: Binding site:216-216 in chain A

UniProt: Binding site:219-219 in chain A

UniProt: Binding site:250-250 in chain B

UniProt: Binding site:252-252 in chain B

UniProt: Binding site:263-263 in chain A

UniProt: Binding site:33-33 in chain A

UniProt: Binding site:330-330 in chain A

UniProt: Binding site:331-331 in chain A

UniProt: Binding site:338-338 in chain B

UniProt: Binding site:416-416 in chain A

UniProt: Binding site:85-85 in chain A

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_A0A0H3GLK6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3188	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

PDC PDB via homolog 167.1 Da · LogP 0.48 · TPSA 87.5 Open detail RCSB PDB

SAJ PDB via homolog Detail RCSB PDB

UGA PDB via homolog Detail RCSB PDB

UPG PDB via homolog Detail RCSB PDB

ZINC34049460 ZINC proposed compound · Tanimoto 0.762 Detail ZINC

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
PDC RCSB PDB	3OJO	P95708	167.1 Da LogP 0.48 TPSA 87.5	✓ Ro5	✓ Clean	`c1cc(nc(c1)C(=O)O)C(=O)O`
SAJ RCSB PDB	4R16	O59284	621.3 Da LogP -4.56 TPSA 322.9	3 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H]([C@@H]([C@H](O[C@@H]1OP(=O)(…`
UGA RCSB PDB	3GG2	Q7MVC7	580.3 Da LogP -4.70 TPSA 314.1	3 viol.	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
UPG RCSB PDB	3VTF	A1RUM9	566.3 Da LogP -4.79 TPSA 297.0	3 viol.	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`

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
ZINC34049460 ZINC	0.762	244.2 Da LogP 1.54 TPSA 100.4	✓ Ro5	✓ Clean	`O=C(O)c1cccc(-c2cccc(C(=O)O)n2)n1`
ZINC13548378 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC21990496 ZINC	0.727	321.3 Da LogP 2.60 TPSA 113.3	✓ Ro5	✓ Clean	`O=C(O)c1cccc(-c2cccc(-c3cccc(C(=O)O)n3)n2)n1`
ZINC331827 ZINC	0.696	202.0 Da LogP 1.54 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1cccc(Br)n1`
ZINC4352696 ZINC	0.696	249.0 Da LogP 1.38 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1cccc(I)n1`
ZINC12959005 ZINC	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC12959016 ZINC	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@](=O)(O)O[P@](=O)(O…`
ZINC25726233 ZINC	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC3861755 ZINC	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875255 ZINC	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875256 ZINC	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)…`
ZINC3875257 ZINC	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875258 ZINC	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)…`
ZINC88466482 ZINC	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC35636069 ZINC	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)OP(=O)(O)O)[…`
ZINC40655887 ZINC	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)OP(=O)(O)O)[…`
ZINC40655889 ZINC	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC44460318 ZINC	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC4490939 ZINC	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585026 ZINC	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585028 ZINC	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O…`
ZINC8585030 ZINC	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585032 ZINC	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O…`
ZINC308666757 ZINC	0.680	219.1 Da LogP 1.52 TPSA 67.3	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)C(F)(F)F)n1`
ZINC102211562 ZINC	0.667	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC110347779 ZINC	0.667	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC110347782 ZINC	0.667	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC97976147 ZINC	0.667	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC98175528 ZINC	0.640	240.5 Da LogP 2.61 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(Cl)(Cl)Cl)n1`
ZINC34563915 ZINC	0.630	222.2 Da LogP 1.26 TPSA 70.5	✓ Ro5	✓ Clean	`CCN(CC)C(=O)c1cccc(C(=O)O)n1`
ZINC36756657 ZINC	0.630	220.2 Da LogP 1.02 TPSA 70.5	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)N2CCCC2)n1`
ZINC12503831 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]2…`
ZINC12503833 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H]…`
ZINC13512000 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC1532538 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC2026984 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC2123545 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC2606131 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC36377965 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC3870257 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC3870258 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC3870259 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC3870260 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC9235501 ZINC	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H…`
ZINC2566954 ZINC	0.615	203.2 Da LogP 0.03 TPSA 104.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc(S(=O)(=O)O)n1`
ZINC174780 ZINC	0.607	209.2 Da LogP 1.34 TPSA 76.5	✓ Ro5	✓ Clean	`CC(C)OC(=O)c1cccc(C(=O)O)n1`
ZINC21161893 ZINC	0.607	223.2 Da LogP 1.74 TPSA 76.5	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)c1cccc(C(=O)O)n1`
ZINC218535275 ZINC	0.607	224.2 Da LogP -0.41 TPSA 116.6	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)c1cccc(C(=O)O)n1`
ZINC36756666 ZINC	0.607	208.2 Da LogP 0.92 TPSA 79.3	✓ Ro5	✓ Clean	`CC(C)NC(=O)c1cccc(C(=O)O)n1`
ZINC220143873 ZINC	0.603	486.1 Da LogP -1.52 TPSA 244.1	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=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 A0A0H3GLK6