KpATCC43816 Protein target profile

glycogen debranching enzyme GlgX

Accession: VK055_3674

Gene: AIK82229.1 glgX 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GYH9

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Length 658

Pocket druggability (P2Rank · AlphaFold DB model) 0.871

Direct ligand evidence 0 54 total records

Functional annotation 1 EC 7 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

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.87. Structure available AlphaFold DB model + ColabFold model 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 (%): 45.122 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.46 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) 0.871

Structure A0A0H3GYH9

Pocket Pocket 1

Druggability (FPocket) 0.651

Structure A0A0H3GYH9

Pocket Pocket 8

ColabFold model

P2Rank 0.922 · Pocket 1

FPocket 0.604 · Pocket 4

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 131 / 4744 genomes with a hit

Prevalence 2.8%

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.

MTSLAAGKPAPLGASYDGKGVNFALFSAHAERVELCVFDEQGNEQRFDLPARSGDIWHGWLAAAGPGLRYGYRVHGPWDPAQGHRFNPAKLLIDPSAHRVEGDLPDDERLHGGMWQPDRRDSAAVAPKSQVVDLRYDWRGDKPPRTPWGETVIYEAHVKGLTLLNPQLPEAIRGTYKALGHPAMIAYFKSLGISALELLPVAQFASEPRLQRMGLSNYWGYNPLAWFALDPRYASDPDRALDEFRDAVKALHAAGIEVILDIVLNHSAEIDLEGPTVSLRGIDNRSYYWVREDGDYHNWTGCGNTLNLSHPGVVEWARQCLRFWVDECHVDGFRFDLASVMGRTPEFRQDAPLFEAIRRDSVLSQVKLIAEPWDIGPGGYQVGNFPPLFAEWNDHFRDSARRFWLQQNVSLGDFAQRFAASSDLFARDGKPPSATVNLVTAHDGFTLRDCVCFNQKHNEANGEENRDGTNNNYSNNHGIEGLEANFAVIERRRASAHALLTTLLLAQGTPMLLAGDEQGHSQHGNNNAYCQDNALTWLDWRQANPGLTAFTAALIHLRRRIPALTRNRWWQEGDGNVRWLNRNAQPLTAAEWQQGAACMQIQLSDRWLLTLNATAEVVDMVLPEGEWRAVPPFAGEDNPVIMAVWHGPAHGVCVFQRS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

3.2.1.196

Gene Ontology (GO)

GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
GO:0004133 OBSOLETE. Catalysis of the cleavage of branch points in branched glycogen polymers.
GO:0005977 The chemical reactions and pathways involving glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues in alpha-(1->4) glycosidic linkage, joined together by alpha-(1->6) glycosidic linkages.
GO:0005980 The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
GO:0004553 Catalysis of the hydrolysis of any O-glycosyl bond.
GO:0004135 Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin. Limit dextrin is the highly branched core that remains after exhaustive treatment of glycogen with glycogen phosphorylase. It is formed because these enzymes cannot hydrolyze the (1->6) glycosidic linkages present.
GO:0120549 Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit dextrin.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
130	558	SMART	SM00642	aamy
130	558	InterPro	IPR006047	Glycosyl hydrolase, family 13, catalytic domain
135	565	SUPERFAMILY	SSF51445	(Trans)glycosidases
135	565	InterPro	IPR017853	Glycoside hydrolase superfamily
571	655	Pfam	PF18390	Glycogen debranching enzyme C-terminal domain
571	655	InterPro	IPR040784	Glycogen debranching enzyme, C-terminal domain
135	572	Gene3D	G3DSA:3.20.20.80	Glycosidases
3	657	Hamap	MF_01248	Glycogen debranching enzyme [glgX].
3	657	InterPro	IPR022844	Glycogen debranching enzyme, bacterial
11	96	Pfam	PF02922	Carbohydrate-binding module 48 (Isoamylase N-terminal domain)
11	96	InterPro	IPR004193	Glycoside hydrolase, family 13, N-terminal
185	287	Pfam	PF00128	Alpha amylase, catalytic domain
185	287	InterPro	IPR006047	Glycosyl hydrolase, family 13, catalytic domain
7	634	NCBIfam	TIGR02100	glycogen debranching protein GlgX
7	634	InterPro	IPR011837	Glycogen debranching enzyme, GlgX type
1	133	Gene3D	G3DSA:2.60.40.10	Immunoglobulins
1	133	InterPro	IPR013783	Immunoglobulin-like fold
4	626	PANTHER	PTHR43002	GLYCOGEN DEBRANCHING ENZYME
573	657	Gene3D	G3DSA:2.60.40.1180	-
573	657	InterPro	IPR013780	Glycosyl hydrolase, all-beta
136	561	CDD	cd11326	AmyAc_Glg_debranch
11	133	CDD	cd02856	E_set_GDE_Isoamylase_N
11	133	InterPro	IPR044505	Glycogen debranching enzyme GlgX/isoamylase, N-terminal Early set domain
7	144	SUPERFAMILY	SSF81296	E set domains
7	144	InterPro	IPR014756	Immunoglobulin E-set

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

0.871

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Surrounding area

Pocket 2 P2Rank #2

0.389

Likely same site as FPocket 8 2.2 Å 15 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.26

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Surrounding area

Pocket 4 P2Rank #4

0.207

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Surrounding area

Pocket 5 P2Rank #5

0.125

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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 #8

0.651 Unusual size

Likely same site as P2Rank 2 2.2 Å 15 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #7

0.583

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Surrounding area

Residue sets

UniProt: Active site:336-336 Nucleophile

UniProt: Active site:371-371 Proton donor

UniProt: Site:443-443 Transition state stabilizer

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.922

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Surrounding area

Pocket 2 P2Rank #2

0.323

Likely same site as FPocket 4 1.6 Å 18 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.291

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Surrounding area

Pocket 4 P2Rank #4

0.168

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Surrounding area

Pocket 5 P2Rank #5

0.148

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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 #4

0.604 Unusual size

Likely same site as P2Rank 2 1.6 Å 18 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #18

0.338

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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_A0A0H3GYH9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3674	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

ARE PDB via homolog 807.7 Da · LogP -10.74 · TPSA 400.3 Open detail RCSB PDB

BTB PDB via homolog Detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

TAM PDB via homolog Detail RCSB PDB

ZINC1615342 ZINC proposed compound · Tanimoto 1.000 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
ARE RCSB PDB	3A6O	Q08751	807.7 Da LogP -10.74 TPSA 400.3	3 viol.	✓ Clean	`C[C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O[C@@H]2[C@…`
BTB RCSB PDB	3M07	Q8ZPF0	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
FLC RCSB PDB	3VGB	Q55088	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
TAM RCSB PDB	6JFJ	A0A0C5GWS2	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`

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
ZINC1615342 ZINC	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC2575038 ZINC	0.625	205.3 Da LogP 0.00 TPSA 86.7	✓ Ro5	✓ Clean	`NC(CCCO)(CCCO)CCCO`
ZINC100055151 ZINC	0.544	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@H](O[C@H]2[C@H](O[C@@H]3[C@@H](CO)O…`
ZINC100055153 ZINC	0.544	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@H](O[C@H]2[C@H](O[C@@H]3[C@@H](CO)O…`
ZINC2362797719 ZINC	0.544	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@H]2[C@H](O[C@H]3[C@@H](O)[C…`
ZINC55537584 ZINC	0.544	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@H]2[C@H](O[C@@H]3[C@@H](CO)…`
ZINC103664702 ZINC	0.526	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@@H]2[C@@H](O)[C@@H](O)O[C@H…`
ZINC103664705 ZINC	0.526	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@@H]2[C@@H](O)[C@H](O)O[C@H]…`
ZINC1857787936 ZINC	0.522	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@@H](N[C@@H]2C[C@@H](CO)[C@H](O[C@H]3O[…`
ZINC2053528368 ZINC	0.522	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…`
ZINC2053528371 ZINC	0.522	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…`
ZINC2053528373 ZINC	0.522	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…`
ZINC2053528375 ZINC	0.522	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…`
ZINC8437016 ZINC	0.522	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@H](N[C@H]2C[C@H](CO)[C@@H](O[C@@H]3O[C…`
ZINC2334905 ZINC	0.522	261.4 Da LogP 1.10 TPSA 63.9	✓ Ro5	✓ Clean	`CC(C)CCN(CCC(C)C)C(CO)(CO)CO`
ZINC3159953 ZINC	0.522	261.4 Da LogP 1.38 TPSA 63.9	✓ Ro5	✓ Clean	`CCCCCN(CCCCC)C(CO)(CO)CO`
ZINC100055156 ZINC	0.517	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](CO)O[C@@H…`
ZINC100055157 ZINC	0.517	488.4 Da LogP -6.55 TPSA 248.4	2 viol.	✓ Clean	`C[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](CO)O[C@@H…`
ZINC101411483 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@@H]1O[C@H…`
ZINC13536670 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O[C@@H]2[C@@H](CO)O[C@H](O)[C@@…`
ZINC13542690 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@H](O)[C@@H…`
ZINC13549339 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@H]1O[C@@H…`
ZINC16051576 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O[C@H]2[C@@H](CO)O[C@@H](O)[C@H…`
ZINC169619623 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@@H]1O[C@H…`
ZINC202563257 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@@H…`
ZINC21984931 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@H](O)[C@@H](O)[C@@H](O)[C@@H]1O[C@@…`
ZINC2382416918 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C@@H]1O[C…`
ZINC2382416919 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O[C@@H]2[C@H](CO)O[C@@H](O)[C@@…`
ZINC2382416920 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C@@H]1O[C…`
ZINC2383776698 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O[C@H]2[C@H](CO)O[C@@H](O)[C@@…`
ZINC2383776699 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O[C@H]2[C@H](CO)O[C@@H](O)[C@@…`
ZINC238735529 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C@@H]1O[C@…`
ZINC245204744 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O[C@@H]2[C@H](CO)O[C@H](O)[C@H…`
ZINC253530326 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@H…`
ZINC257362198 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@H]…`
ZINC257362199 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@H]…`
ZINC26892042 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C@@H]1O[C@…`
ZINC33821316 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@H]2[C@@H](CO)O[C@@H](O)[C@H]…`
ZINC35262676 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@@…`
ZINC38599730 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@H]…`
ZINC38792149 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O[C@H]2[C@@H](CO)O[C@H](O)[C@H]…`
ZINC40401145 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O[C@H…`
ZINC4095761 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O[C@@…`
ZINC4095762 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@@H](O)[C@H…`
ZINC4097113 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O[C@@H]2[C@@H](CO)O[C@@H](O)[C@…`
ZINC4261772 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@@…`
ZINC43505220 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@H]1O[C@H]…`
ZINC5222464 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C@H]1O[C@H…`
ZINC72283167 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@H]1O[C@H]…`
ZINC958527474 ZINC	0.509	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@H]1O[C@@H…`

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 A0A0H3GYH9