KpATCC43816 Protein target profile

rod shape-determining protein RodA

Accession: VK055_1866

Gene: AIK80472.1 mrdB 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GLD1

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Length 370

Pocket druggability (P2Rank · AlphaFold DB model) 0.74

Direct ligand evidence 0 51 total records

Functional annotation 1 EC 9 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 0.74. 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: 4.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 95.946 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 85.11 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) 0.74

Structure A0A0H3GLD1

Pocket Pocket 1

Druggability (FPocket) 0.951

Structure A0A0H3GLD1

Pocket Pocket 16

ColabFold model

P2Rank 0.62 · Pocket 1

FPocket 0.961 · Pocket 19

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 193 / 4744 genomes with a hit

Prevalence 4.1%

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.

MTDNPNKKSLWDKIHLDPTMLLILLALLTYSALVIWSASGQDVGMMERKIGQIAMGVVIMIVMAQIPPRVYEGWAPYLYIFCIILLVAVDAFGAISKGAQRWLDLGIVRFQPSEIAKIAVPLMVARFINRDVCPPSLKNTGIALVLIFLPTLLVAAQPDLGTSILIALSGLFVLFLSGLSWRLIGIAVVLVAAFIPILWFFLMHDYQRQRVMMLLDPETDPLGAGYHIIQSKIAIGSGGLRGKGWLHGTQSQLEFLPERHTDFIFAVLAEELGLIGVLILLALYILLIMRGLWIAAQAQTTFGRVMAGGLMLILFVYVFVNIGMVSGILPVVGVPLPLVSYGGSALIVLMAGFGIVMSIHTHRKMLSKSV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

2.4.99.28

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
GO:0008360 Any process that modulates the surface configuration of a cell.
GO:0032153 The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
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:0015648 Enables the directed movement of lipid-linked peptidoglycans into, out of or within a cell, or between cells.
GO:0008955 Catalysis of the reaction: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H+.
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:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
263	289	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
74	95	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
321	345	ProSitePatterns	PS00428	Cell cycle proteins ftsW / rodA / spoVE signature.
321	345	InterPro	IPR018365	Cell cycle, FtsW / RodA / SpoVE, conserved site
177	182	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
181	203	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
20	38	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
272	294	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
338	359	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
39	49	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
77	99	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
69	73	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
360	370	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
50	68	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
50	67	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
12	366	Hamap	MF_02079	Peptidoglycan glycosyltransferase MrdB [mrdB].
12	366	InterPro	IPR011923	Probable peptidoglycan glycosyltransferase RodA/MrdB
306	328	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
136	154	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
338	360	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
15	37	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
96	135	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
310	332	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
183	202	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	19	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
333	337	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
20	364	Pfam	PF01098	Cell cycle protein
20	364	InterPro	IPR001182	Probable peptidoglycan glycosyltransferase FtsW/RodA
7	365	PANTHER	PTHR30474	CELL CYCLE PROTEIN
7	365	InterPro	IPR001182	Probable peptidoglycan glycosyltransferase FtsW/RodA
160	179	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
155	159	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
136	155	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
203	262	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
290	309	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
160	176	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
17	364	NCBIfam	TIGR02210	rod shape-determining protein RodA
17	364	InterPro	IPR011923	Probable peptidoglycan glycosyltransferase RodA/MrdB

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

0.74

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Surrounding area

Pocket 2 P2Rank #2

0.411

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Surrounding area

Pocket 3 P2Rank #3

0.157

Likely same site as FPocket 16 2.5 Å 12 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.051

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Surrounding area

Pocket 5 P2Rank #5

0.03

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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 #16

0.951 Unusual size

Likely same site as P2Rank 3 2.5 Å 12 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #1

0.236

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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

0.62

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Surrounding area

Pocket 2 P2Rank #2

0.476

Likely same site as FPocket 7 6.7 Å 5 shared residues 62% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.132

Likely same site as FPocket 19 3.0 Å 9 shared residues 90% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.094

Likely same site as FPocket 1 3.2 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.023

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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 #19

0.961 Unusual size

Likely same site as P2Rank 3 3.0 Å 9 shared residues 90% of smaller site

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Surrounding area

Pocket 2 FPocket #1

0.741

Likely same site as P2Rank 4 3.2 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 3 FPocket #7

0.347

Likely same site as P2Rank 2 6.7 Å 5 shared residues 62% of smaller site

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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_A0A0H3GLD1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1866	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.

51 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 1 records from similar proteins

Structural ligands 1 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

OLC PDB via homolog 356.5 Da · LogP 4.92 · TPSA 66.8 Open detail RCSB PDB

ZINC1501016272 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1501016273 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1501016315 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1501016316 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
OLC RCSB PDB	6BAR	Q5SIX3	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](CO)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
ZINC1501016272 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC1501016273 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC1501016315 ZINC	1.000	314.5 Da LogP 3.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC1501016316 ZINC	1.000	314.5 Da LogP 3.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC2038077522 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2038077523 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC221534416 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OC[C@@H](O)CO`
ZINC32840893 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840894 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840895 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840896 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840901 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840902 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840903 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840904 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC725433050 ZINC	1.000	342.5 Da LogP 4.53 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC725433052 ZINC	1.000	342.5 Da LogP 4.53 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC98208566 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OC[C@H](O)CO`
ZINC32840885 ZINC	0.943	300.4 Da LogP 3.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2053467566 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC=CCC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2053467567 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC=CCC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC29045599 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC4557100 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC4557101 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC5819989 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC5819990 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC85425978 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC29045446 ZINC	0.892	352.5 Da LogP 4.47 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\C/C=C\CCCCC(=O)OC[C@@H](O)CO`
ZINC13532428 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC13532431 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)C/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC13532435 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC13546140 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC13546141 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC2296552808 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)CC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC2296552809 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)CC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC33832849 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC35052109 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC4411072 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)CC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC4411074 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)CC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2516269 ZINC	0.824	246.3 Da LogP 2.02 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840883 ZINC	0.824	302.5 Da LogP 3.58 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840884 ZINC	0.824	302.5 Da LogP 3.58 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840889 ZINC	0.824	316.5 Da LogP 3.97 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840890 ZINC	0.824	316.5 Da LogP 3.97 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840891 ZINC	0.824	330.5 Da LogP 4.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840892 ZINC	0.824	330.5 Da LogP 4.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC72400435 ZINC	0.824	344.5 Da LogP 4.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC77313111 ZINC	0.824	344.5 Da LogP 4.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC8437476 ZINC	0.824	274.4 Da LogP 2.80 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC8437478 ZINC	0.824	274.4 Da LogP 2.80 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[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 A0A0H3GLD1