KpATCC43816 Protein target profile

mannitol dehydrogenase Rossmann domain protein

Accession: VK055_0913

Gene: AIK79536.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GSI7

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Length 487

Pocket druggability (P2Rank · AlphaFold DB model) 0.92

Direct ligand evidence 0 52 total records

Functional annotation 0 EC 4 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 0.92. 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: 2.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 27.374 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 96.75 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) 0.92

Structure A0A0H3GSI7

Pocket Pocket 1

Druggability (FPocket) 0.809

Structure A0A0H3GSI7

Pocket Pocket 18

ColabFold model

P2Rank 0.92 · Pocket 1

FPocket 0.735 · Pocket 9

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 104 / 4744 genomes with a hit

Prevalence 2.2%

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.

MENTLLTANATLPTYDRSALIPRIVHLGFGAFHRAHQAVYADILASEHGSDWGYTEVNLIGGEQQIADLQQQDLLYTVAEMSADAWTARVVGVVKQALHAGVDGLEAVLAAMCQPQVAIVSLTITEKGYCHSPASGELQLDHPLIAADLHNPHQPKSAAGVVVEALSRRRAAGLPAFTVMSCDNMPENGHVMRNVVCAYARALDEDLAAWIEQNVTFPSTMVDRIVPAVTAETLDKITQLTGVRDPAGVACEPFRQWVIEDNFVAGRPQWEKAGAELVADVVPFEEMKLRMLNGSHSFLAYLGYLAGYQHINDCMQDDNYRRAALSLMLDEQAPTLKVQGVDLSRYASLLIDRYCNPALKHRTWQIAMDGSQKLPQRMLDSIRWHLVHQRDFTLLALGVAGWMRYVGGVDDAGQAIEICDPLLPVIQQAVAASADGEARVKALLGIEAIFGVELPQESRFVTAVTRAYLALQRQGAKATVATWAAAQ

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0019594 The chemical reactions and pathways involving mannitol, the alditol derived from D-mannose by reduction of the aldehyde group.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
279	486	Gene3D	G3DSA:1.10.1040.10	-
279	486	InterPro	IPR013328	6-phosphogluconate dehydrogenase, domain 2
23	185	Pfam	PF01232	Mannitol dehydrogenase Rossmann domain
23	185	InterPro	IPR013131	Mannitol dehydrogenase, N-terminal
5	484	PANTHER	PTHR43362	MANNITOL DEHYDROGENASE DSF1-RELATED
4	278	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
4	278	InterPro	IPR036291	NAD(P)-binding domain superfamily
5	278	Gene3D	G3DSA:3.40.50.720	-
2	278	FunFam	G3DSA:3.40.50.720:FF:000129	D-mannonate oxidoreductase
176	189	PRINTS	PR00084	Mannitol dehydrogenase signature
176	189	InterPro	IPR000669	Mannitol dehydrogenase
24	34	PRINTS	PR00084	Mannitol dehydrogenase signature
24	34	InterPro	IPR000669	Mannitol dehydrogenase
215	228	PRINTS	PR00084	Mannitol dehydrogenase signature
215	228	InterPro	IPR000669	Mannitol dehydrogenase
245	260	PRINTS	PR00084	Mannitol dehydrogenase signature
245	260	InterPro	IPR000669	Mannitol dehydrogenase
280	482	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
280	482	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
215	227	ProSitePatterns	PS00974	Mannitol dehydrogenases signature.
215	227	InterPro	IPR023027	Mannitol dehydrogenase, conserved site
213	458	Pfam	PF08125	Mannitol dehydrogenase C-terminal domain
213	458	InterPro	IPR013118	Mannitol dehydrogenase, C-terminal

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

0.92

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Surrounding area

Pocket 2 P2Rank #2

0.127

Likely same site as FPocket 18 2.6 Å 8 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.082

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Surrounding area

Pocket 4 P2Rank #4

0.058

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Surrounding area

Pocket 5 P2Rank #5

0.024

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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

0.809 Unusual size

Likely same site as P2Rank 2 2.6 Å 8 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.92

Likely same site as FPocket 9 7.0 Å 16 shared residues 84% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.115

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Surrounding area

Pocket 3 P2Rank #3

0.024

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Surrounding area

Pocket 4 P2Rank #4

0.017

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Surrounding area

Pocket 5 P2Rank #5

0.014

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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_A0A0H3GSI7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0913	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

CS2 PDB via homolog 196.2 Da · LogP -3.49 · TPSA 138.5 Open detail RCSB PDB

MTL PDB via homolog Detail RCSB PDB

ZINC1531007 ZINC proposed compound · Tanimoto 0.950 Detail ZINC

ZINC100064885 ZINC proposed compound · Tanimoto 0.917 Detail ZINC

ZINC4403107 ZINC proposed compound · Tanimoto 0.917 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
CS2 RCSB PDB	4IM7	A0A0H2V7F2	196.2 Da LogP -3.49 TPSA 138.5	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H]([C@@H](C(=O)O)O)O)O)O)O`
MTL RCSB PDB	1M2W	O08355	182.2 Da LogP -3.59 TPSA 121.4	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H]([C@@H](CO)O)O)O)O)O`

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
ZINC1531007 ZINC	0.950	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)…`
ZINC100064885 ZINC	0.917	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC4403107 ZINC	0.917	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@…`
ZINC9212412 ZINC	0.917	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)C(O)[C@H](O)[C@@H](O)CO`
ZINC5201837 ZINC	0.647	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@H](…`
ZINC5201838 ZINC	0.647	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@@H]…`
ZINC5201839 ZINC	0.647	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@H](…`
ZINC5201841 ZINC	0.647	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@@H]…`
ZINC12359024 ZINC	0.632	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.632	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.632	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.632	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.632	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.632	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.632	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.632	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.632	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC101356848 ZINC	0.579	388.4 Da LogP -6.96 TPSA 226.4	2 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)CNCCNC[C@H](O…`
ZINC215968865 ZINC	0.579	388.4 Da LogP -6.96 TPSA 226.4	2 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)CNCCNC[C@H](O…`
ZINC215968917 ZINC	0.579	388.4 Da LogP -6.96 TPSA 226.4	2 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)CNCCNC[C@H](O…`
ZINC215968963 ZINC	0.579	388.4 Da LogP -6.96 TPSA 226.4	2 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CNCCNC[C@@H…`
ZINC216185927 ZINC	0.579	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC216185976 ZINC	0.579	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC216186168 ZINC	0.579	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC216186206 ZINC	0.579	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC25624721 ZINC	0.579	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC25624980 ZINC	0.579	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC4566610 ZINC	0.579	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC4566614 ZINC	0.579	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC100055463 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC100056793 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC113074329 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC12953162 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC12953168 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC13522684 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)CO`
ZINC14944599 ZINC	0.550	256.4 Da LogP -0.11 TPSA 80.9	✓ Ro5	✓ Clean	`CCSC(SCC)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC17780060 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@@H](O)[C@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC17952732 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC18042331 ZINC	0.550	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H]…`
ZINC18120313 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC3979006 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC4353160 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)CO`
ZINC4353166 ZINC	0.550	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353168 ZINC	0.550	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4403103 ZINC	0.550	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC4403105 ZINC	0.550	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC4521296 ZINC	0.550	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H]…`
ZINC95884213 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC9915770 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC9915771 ZINC	0.550	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`

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 A0A0H3GSI7