KpATCC43816 Protein target profile

NAD-dependent glycerol-3-phosphate dehydrogenasefamily protein

Accession: VK055_0795

Gene: AIK79418.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GNC1

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Length 291

Pocket druggability (P2Rank · AlphaFold DB model) 0.915

Direct ligand evidence 0 60 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

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.92, FPocket 0.92). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.92. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.92. 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: Hit
Human identity (%): 29.021 Lower values reduce human off-target concern.
Human E-value: 2.21e-32
Gut microbiome similarity: 0.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 25.952 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 96.51 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) 0.915

Structure A0A0H3GNC1

Pocket Pocket 1

Druggability (FPocket) 0.917

Structure A0A0H3GNC1

Pocket Pocket 7

ColabFold model

P2Rank 0.904 · Pocket 1

FPocket 0.915 · Pocket 11

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 18 / 4744 genomes with a hit

Prevalence 0.4%

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.

MSTLPKVAVLGLGAMGHAFASNLLKNGFTVAGWNRSPARGEDLQAHGLSLHATPQQSVADAEVIISMLADGEATLEVLAQIAPACQPQAIYCQMGTIGLPETRQAIALLRELQPAMTYIDAPVSGTKAPAEKAQILVLASGDREKGAAAEPVFAAISRGTQWFGEAGNSQKMKLVLNAWLISMMQGIAESAQLAKTLGFTPDQLWSALEGGPLAAPYVKVKLDAIASEQFTPQMQLAHALKDARLALSLAEPHTMPGLETIAELWQQAADAGYAGEDLSAVYQWLSPSSKA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: Periplasmic

Gene Ontology (GO)

GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
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: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.

21 records

Show feature table

Start	End	DB	Term	Name
1	164	Gene3D	G3DSA:3.40.50.720	-
165	286	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
165	286	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region
7	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
16	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
166	290	Gene3D	G3DSA:1.10.1040.10	-
166	290	InterPro	IPR013328	6-phosphogluconate dehydrogenase, domain 2
4	284	PANTHER	PTHR43580	OXIDOREDUCTASE GLYR1-RELATED
167	285	Pfam	PF14833	NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase
167	285	InterPro	IPR029154	3-hydroxyisobutyrate dehydrogenase-like, NAD-binding domain
1	20	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
1	20	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
21	291	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
6	165	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
6	165	InterPro	IPR036291	NAD(P)-binding domain superfamily
6	162	Pfam	PF03446	NAD binding domain of 6-phosphogluconate dehydrogenase
6	162	InterPro	IPR006115	6-phosphogluconate dehydrogenase, NADP-binding
1	6	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
1	291	PIRSF	PIRSF000103	HIBADH
1	291	InterPro	IPR015815	3-hydroxyisobutyrate dehydrogenase-related

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

0.915

Show in viewer

Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #7

0.917

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:173-173

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #11

0.915

Show in viewer

Surrounding area

Pocket 2 FPocket #12

0.571

Show in viewer

Surrounding area

Pocket 3 FPocket #7

0.328

Show in viewer

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_A0A0H3GNC1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0795	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.

60 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3OH PDB via homolog 90.1 Da · LogP -0.55 · TPSA 57.5 Open detail RCSB PDB

9ON PDB via homolog Detail RCSB PDB

AKR PDB via homolog Detail RCSB PDB

BO3 PDB via homolog Detail RCSB PDB

HIU PDB via homolog Detail RCSB PDB

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
3OH RCSB PDB	5Y8O	P9WNY5	90.1 Da LogP -0.55 TPSA 57.5	✓ Ro5	✓ Clean	`C(CO)C(=O)O`
9ON RCSB PDB	5Y8L	P9WNY5	146.1 Da LogP 0.57 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)C(=O)O`
AKR RCSB PDB	5Y8M	P9WNY5	72.1 Da LogP 0.26 TPSA 37.3	✓ Ro5	✓ Clean	`C=CC(=O)O`
BO3 RCSB PDB	6SM7	P0A9V8	61.8 Da LogP -2.05 TPSA 60.7	✓ Ro5	✓ Clean	`B(O)(O)O`
HIU RCSB PDB	5Y8M	P9WNY5	104.1 Da LogP -0.30 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](CO)C(=O)O`
HUI RCSB PDB	5Y8L	P9WNY5	104.1 Da LogP -0.30 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](CO)C(=O)O`
LLQ RCSB PDB	6SMY	P0A9V8	156.2 Da LogP -1.77 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@@H](CS(=O)(=O)O)O)O`
LW7 RCSB PDB	6JIT	D3Q3R0	235.3 Da LogP 3.66 TPSA 12.4	✓ Ro5	✓ Clean	`c1ccc(cc1)CCC2=NCCc3c2cccc3`
LW9 RCSB PDB	6JIZ	D3Q3R0	128.3 Da LogP 3.61 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCC(CC)CC`
TLA RCSB PDB	5XVH	A3MU08	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=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
ZINC4578142 ZINC	0.727	221.3 Da LogP 3.27 TPSA 12.4	✓ Ro5	✓ Clean	`c1ccc(CC2=NCCc3ccccc32)cc1`
ZINC12359024 ZINC	0.692	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	0.692	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	0.692	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	0.692	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	0.692	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	0.692	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	0.692	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	0.692	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	0.692	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`
ZINC220366073 ZINC	0.619	214.4 Da LogP 4.66 TPSA 9.2	✓ Ro5	✓ Clean	`CCCC[C@@H](CC)COCC(CC)CC`
ZINC220366143 ZINC	0.619	214.4 Da LogP 4.66 TPSA 9.2	✓ Ro5	✓ Clean	`CCCC[C@H](CC)COCC(CC)CC`
ZINC4956068 ZINC	0.610	295.4 Da LogP 3.68 TPSA 30.8	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)C(CCc1ccccc1)=NCC2`
ZINC2029340 ZINC	0.591	216.3 Da LogP 2.38 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029341 ZINC	0.591	216.3 Da LogP 2.38 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@H](CCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029343 ZINC	0.591	216.3 Da LogP 2.38 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCC[C@H](C)C(=O)O)C(=O)O`
ZINC2029346 ZINC	0.591	230.3 Da LogP 2.77 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029348 ZINC	0.591	230.3 Da LogP 2.77 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@H](CCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029350 ZINC	0.591	230.3 Da LogP 2.77 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCC[C@H](C)C(=O)O)C(=O)O`
ZINC2029355 ZINC	0.591	258.4 Da LogP 3.55 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029358 ZINC	0.591	258.4 Da LogP 3.55 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@H](CCCCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029360 ZINC	0.591	258.4 Da LogP 3.55 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCCCC[C@H](C)C(=O)O)C(=O)O`
ZINC2383325707 ZINC	0.591	213.4 Da LogP 4.36 TPSA 26.0	✓ Ro5	✓ Clean	`CCCCC(CCCC)C[C@@H](CC)CN`
ZINC2383325708 ZINC	0.591	213.4 Da LogP 4.36 TPSA 26.0	✓ Ro5	✓ Clean	`CCCCC(CCCC)C[C@H](CC)CN`
ZINC4100991 ZINC	0.591	286.4 Da LogP 4.33 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC4100995 ZINC	0.591	286.4 Da LogP 4.33 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@H](CCCCCCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC4101001 ZINC	0.591	286.4 Da LogP 4.33 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCCCCCC[C@H](C)C(=O)O)C(=O)O`
ZINC1560405156 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC85409934 ZINC	0.579	223.3 Da LogP 2.02 TPSA 16.2	✓ Ro5	✓ Clean	`c1cc[n+](CC2=NCCc3ccccc32)cc1`
ZINC190736 ZINC	0.575	304.3 Da LogP 2.72 TPSA 49.7	✓ Ro5	✓ Clean	`O=C1c2ccccc2C(=O)N1CCC1=NCCc2ccccc21`
ZINC5120949 ZINC	0.575	256.3 Da LogP 1.57 TPSA 49.7	✓ Ro5	✓ Clean	`O=C1CCC(=O)N1CCC1=NCCc2ccccc21`
ZINC142127993 ZINC	0.571	219.2 Da LogP -1.20 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](O)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC214811896 ZINC	0.571	219.2 Da LogP -1.20 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@H](O)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC214811946 ZINC	0.571	219.2 Da LogP -1.20 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](O)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC214811999 ZINC	0.571	219.2 Da LogP -1.20 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@H](O)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC13529664 ZINC	0.560	320.3 Da LogP -1.08 TPSA 190.3	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=…`
ZINC14510370 ZINC	0.556	244.4 Da LogP 3.74 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCO`
ZINC1531061 ZINC	0.556	216.3 Da LogP 2.96 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCO`
ZINC1610426 ZINC	0.556	230.3 Da LogP 3.35 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCO`
ZINC2168567 ZINC	0.556	202.3 Da LogP 2.57 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCO`
ZINC3861297 ZINC	0.556	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCO`
ZINC4284502 ZINC	0.556	258.4 Da LogP 4.13 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCO`
ZINC5287109 ZINC	0.556	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCCO`
ZINC2242980 ZINC	0.552	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC2560662 ZINC	0.552	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC5360219 ZINC	0.552	231.2 Da LogP 0.47 TPSA 103.7	✓ Ro5	✓ Clean	`CC(C)CC(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC2570024 ZINC	0.545	214.4 Da LogP 4.54 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@H](CC)CO`
ZINC2600052 ZINC	0.545	214.4 Da LogP 4.54 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@@H](CC)CO`
ZINC2171316 ZINC	0.542	214.4 Da LogP 4.39 TPSA 20.2	✓ Ro5	✓ Clean	`CCCC[C@H](CC)CCCC[C@@H](C)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 A0A0H3GNC1