KpATCC43816 Protein target profile

N5-glutamine methyltransferase, ribosomal protein L3-specific

Accession: VK055_4793

Gene: prmB AIK83320.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GVU0

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Length 310

Pocket druggability (P2Rank · AlphaFold DB model) 0.765

Direct ligand evidence 0 51 total records

Functional annotation 1 EC 10 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

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 1 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 (%): 29.004 Lower values reduce human off-target concern.
Human E-value: 2.45e-14
Gut microbiome similarity: 3.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 61.486 Higher values support similarity to known essential genes.
DEG E-value: 6.63e-142 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.89 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) 0.765

Structure A0A0H3GVU0

Pocket Pocket 1

Druggability (FPocket) 0.957

Structure A0A0H3GVU0

Pocket Pocket 1

ColabFold model

P2Rank 0.906 · Pocket 1

FPocket 0.866 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 180 / 4744 genomes with a hit

Prevalence 3.8%

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.

MDKIFVDEAVNELHTIQDMLRWAVSRFSAANIWYGHGTDNPWDEAVQLVLPSLYLPLDIPEDMRTARLTSSEKHRIVERVIRRVNERIPVAYLTNKAWFCGHEFYVDERVLVPRSPIGELINNQFAGLINHKPQHILDMCTGSGCIAIACAYAFPEAEVDAVDISPDALAVAEHNVESHGLIHHVTPIRSDLFRDLPKLQYDLIVTNPPYVDEEDMADLPEEYEHEPVLGLASGSDGLKLTRRILGNAPDYLSDDGILICEVGNSMVHLMEQYPDVPFTWLEFDNGGDGVFMLTKQQLIDARAHFGIYKD

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.1.1.298

Gene Ontology (GO)

GO:0006479 The addition of a methyl group to a protein amino acid. A methyl group is derived from methane by the removal of a hydrogen atom.
GO:0003676 Binding to a nucleic acid.
GO:0008276 Catalysis of the transfer of a methyl group (CH3-) to a protein.
GO:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule.
GO:0009007 Catalysis of the reaction: S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.
GO:0032259 The process in which a methyl group is covalently attached to a molecule.
GO:0032775 OBSOLETE. The covalent transfer of a methyl group to N-6 of adenine in a DNA molecule.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0005840 An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
GO:0036009 Catalysis of the reaction: L-glutaminyl-[protein] + S-adenosyl-L-methionine = N(5)-methyl-L-glutaminyl-[protein] + S-adenosyl-L-homocysteine + H+.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
6	300	Hamap	MF_02125	50S ribosomal protein L3 glutamine methyltransferase [prmB].
6	300	InterPro	IPR017127	Ribosomal protein L3-specific, glutamine-N5-methyltransferase
105	279	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
105	279	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
1	307	PIRSF	PIRSF037167	Mtase_YfcB
1	307	InterPro	IPR017127	Ribosomal protein L3-specific, glutamine-N5-methyltransferase
14	104	Gene3D	G3DSA:1.10.8.10	-
105	279	FunFam	G3DSA:3.40.50.150:FF:000042	50S ribosomal protein L3 glutamine methyltransferase
1	310	PANTHER	PTHR47806	50S RIBOSOMAL PROTEIN L3 GLUTAMINE METHYLTRANSFERASE
1	310	InterPro	IPR017127	Ribosomal protein L3-specific, glutamine-N5-methyltransferase
131	215	Pfam	PF05175	Methyltransferase small domain
131	215	InterPro	IPR007848	Methyltransferase small domain
204	210	ProSitePatterns	PS00092	N-6 Adenine-specific DNA methylases signature.
204	210	InterPro	IPR002052	DNA methylase, N-6 adenine-specific, conserved site
15	293	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
15	293	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
14	104	FunFam	G3DSA:1.10.8.10:FF:000022	50S ribosomal protein L3 glutamine methyltransferase
136	210	CDD	cd02440	AdoMet_MTases
15	302	NCBIfam	TIGR00536	HemK family protein methyltransferase
15	302	InterPro	IPR004556	Methyltransferase HemK-like
13	295	NCBIfam	TIGR03533	50S ribosomal protein L3 N(5)-glutamine methyltransferase
13	295	InterPro	IPR017127	Ribosomal protein L3-specific, glutamine-N5-methyltransferase

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

0.765

Likely same site as FPocket 1 2.0 Å 25 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.377

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Surrounding area

Pocket 3 P2Rank #3

0.009

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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 #1

0.957 Unusual size

Likely same site as P2Rank 1 2.0 Å 25 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

0.906

Likely same site as FPocket 1 2.7 Å 34 shared residues 87% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.016

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Surrounding area

Pocket 3 P2Rank #3

0.002

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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_A0A0H3GVU0	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4793	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

MEQ PDB via homolog 160.2 Da · LogP -1.08 · TPSA 92.4 Open detail RCSB PDB

ZINC1529737 ZINC proposed compound · Tanimoto 0.714 Detail ZINC

ZINC2384790 ZINC proposed compound · Tanimoto 0.714 Detail ZINC

ZINC2560745 ZINC proposed compound · Tanimoto 0.714 Detail ZINC

ZINC2560989 ZINC proposed compound · Tanimoto 0.714 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
MEQ RCSB PDB	1NV8	Q9WYV8	160.2 Da LogP -1.08 TPSA 92.4	✓ Ro5	✓ Clean	`CNC(=O)CC[C@@H](C(=O)O)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
ZINC1529737 ZINC	0.714	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC2384790 ZINC	0.714	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC2560745 ZINC	0.714	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC2560989 ZINC	0.714	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC2390999 ZINC	0.655	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC2516115 ZINC	0.613	246.3 Da LogP -0.60 TPSA 129.7	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC13514803 ZINC	0.606	347.3 Da LogP -1.88 TPSA 196.1	1 viol.	✓ Clean	`C[C@H](NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=…`
ZINC1576202 ZINC	0.600	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)NCC(=O)O)C(=O)O`
ZINC3995565 ZINC	0.600	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)NCC(=O)O)C(=O)O`
ZINC2504764 ZINC	0.594	232.2 Da LogP -0.84 TPSA 129.7	✓ Ro5	✓ Clean	`CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC3055005 ZINC	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007 ZINC	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010 ZINC	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC2391099 ZINC	0.586	274.3 Da LogP -2.59 TPSA 178.6	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC1608689 ZINC	0.576	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCNC(=O)CC[C@H](N)C(=O)O`
ZINC2045835 ZINC	0.576	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCNC(=O)CC[C@@H](N)C(=O)O`
ZINC2384788 ZINC	0.576	260.3 Da LogP -0.21 TPSA 129.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC12496578 ZINC	0.571	275.3 Da LogP -2.12 TPSA 158.8	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC2556600 ZINC	0.567	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)CCC(N)=O)C(=O)O`
ZINC1555366 ZINC	0.565	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1555367 ZINC	0.565	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1555369 ZINC	0.565	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720127 ZINC	0.565	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1720128 ZINC	0.565	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720130 ZINC	0.565	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC13507519 ZINC	0.563	234.2 Da LogP -2.26 TPSA 150.0	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CO)C(=O)O)C(=O)O`
ZINC1576203 ZINC	0.563	261.2 Da LogP -2.50 TPSA 158.8	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)NCC(=O)NCC(=O)O)C(=O)O`
ZINC2516116 ZINC	0.563	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC4545887 ZINC	0.563	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC4545888 ZINC	0.563	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)NCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC4545889 ZINC	0.563	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC1581634 ZINC	0.552	203.2 Da LogP -2.22 TPSA 135.5	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NCC(=O)O`
ZINC5500823 ZINC	0.552	203.2 Da LogP -2.22 TPSA 135.5	✓ Ro5	✓ Clean	`NC(=O)CC[C@@H](N)C(=O)NCC(=O)O`
ZINC2242694 ZINC	0.545	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC2547582 ZINC	0.545	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC3870040 ZINC	0.545	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O`
ZINC3870041 ZINC	0.545	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS)C(=O)O)C(=O)O`
ZINC3870042 ZINC	0.545	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O`
ZINC3870043 ZINC	0.545	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS)C(=O)O)C(=O)O`
ZINC3872193 ZINC	0.545	240.2 Da LogP -1.86 TPSA 146.8	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)NCS(=O)(=O)O)C(=O)O`
ZINC4096970 ZINC	0.545	405.4 Da LogP -2.04 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CCC(=O)N[C@@H](CCC(=O)O)…`
ZINC4545890 ZINC	0.545	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC4545891 ZINC	0.545	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC2560992 ZINC	0.531	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC12954078 ZINC	0.529	222.2 Da LogP 0.82 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)Nc1ccccc1)C(=O)O`
ZINC12954085 ZINC	0.529	222.2 Da LogP 0.82 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)Nc1ccccc1)C(=O)O`
ZINC2106542 ZINC	0.519	245.3 Da LogP 1.99 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCCCCCC(=O)O)C(=O)O`
ZINC2106543 ZINC	0.519	245.3 Da LogP 1.99 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCCCCCC(=O)O)C(=O)O`
ZINC2108713 ZINC	0.519	217.3 Da LogP 1.21 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCCCC(=O)O)C(=O)O`
ZINC2108714 ZINC	0.519	217.3 Da LogP 1.21 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCCCC(=O)O)C(=O)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 A0A0H3GVU0