KpATCC43816 Protein target profile

membrane-bound lytic murein transglycosylase F

Accession: VK055_4617

Gene: yfhD AIK83152.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GW83

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Length 538

Pocket druggability (P2Rank · AlphaFold DB model) 0.873

Direct ligand evidence 0 51 total records

Functional annotation 1 EC 8 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: 2.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 87.06 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) 0.873

Structure A0A0H3GW83

Pocket Pocket 1

Druggability (FPocket) 0.948

Structure A0A0H3GW83

Pocket Pocket 8

ColabFold model

P2Rank 0.878 · Pocket 1

FPocket 0.974 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 115 / 4744 genomes with a hit

Prevalence 2.4%

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.

MPHIRRQPCVFSGHRLLRNLKLQKINSLKKLKINYLLIGIVTLLLAAALWPSIPWSGKPENRVAGIIARGELRISTINSPMTFATMNNKAFGLDYELAKQFADYLGVTLKITVRQNISQLFDDLDDGQADMLAAGLVYNQERVKNYQAGPTYYSVSQQLVYRVGNTRPRTLAALTAEQLTIAPGHVAINDLQTLKAEKYPDLAWRVDEKRGTTALMQAVIDGKLDYTIADSVAVSLFQRVHPELAVALDITDEQPVTWFSARDDDNSLSAAMLDFFNNINEDGTLARLEEKYLGHGNDFDYVDTRTFLRAVENILPEVQPLFEKYAREIDWRLLAAIAWQESHWDPQATSPTGVRGMMMLTRNTAQSLGLTDRTDAAQSIDGGMRYLQDMMDKVPDSIPKDERIWFALAAYNMGYAHMLDAMALTRKQKGNPNSWADVKLRLPLLSQKPYYSKLKYGYARGHEAYAYVENIRKYQISLVGYLSEKERQQQQTLALAEDYPAVLPNELEQPQETTLPFFKFRADKQMDNARMKLPGHLY

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

4.2.2.n1

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0016837 Catalysis of the cleavage of a carbon-oxygen bond by the elimination of an alcohol from a polysaccharide.
GO:0000270 The chemical reactions and pathways involving peptidoglycans, any of a class of glycoconjugates found only 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.
GO:0008933 Catalysis of the cleavage of a peptidoglycan chain into a peptidoglycan chain with N-acetyl-1,6-anhydromuramyl-[peptide] at the reducing end + a peptidoglycan chain with N-acetylglucosamine at the non-reducing end. Includes endolytic transglycosylase activity that fragments the glycan chain internally and exolytic transgylcosylase activity that cleaves a terminal disaccharide from the end of the glycan strand.
GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures.
GO:0016998 The chemical reactions and pathways resulting in the breakdown of macromolecules that form part of a cell wall.
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:0009253 The chemical reactions and pathways resulting in the breakdown 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.

25 records

Show feature table

Start	End	DB	Term	Name
32	499	Hamap	MF_02016	Membrane-bound lytic murein transglycosylase F [mltF].
32	499	InterPro	IPR023703	Membrane-bound lytic murein transglycosylase F
156	252	Gene3D	G3DSA:3.40.190.10	-
322	479	CDD	cd13403	MLTF-like
70	294	CDD	cd01009	PBP2_YfhD_N
337	365	ProSitePatterns	PS00922	Prokaryotic transglycosylases signature.
337	365	InterPro	IPR000189	Prokaryotic transglycosylase, active site
1	32	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
71	296	SMART	SM00062	AABind_6
71	296	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
156	252	FunFam	G3DSA:3.40.190.10:FF:000051	Membrane-bound lytic murein transglycosylase F
66	290	Gene3D	G3DSA:3.40.190.10	-
33	429	PANTHER	PTHR35936	MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F
299	479	FunFam	G3DSA:1.10.530.10:FF:000003	Membrane-bound lytic murein transglycosylase F
33	55	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
68	296	SUPERFAMILY	SSF53850	Periplasmic binding protein-like II
54	538	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
33	53	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
78	295	Pfam	PF00497	Bacterial extracellular solute-binding proteins, family 3
78	295	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
273	468	SUPERFAMILY	SSF53955	Lysozyme-like
273	468	InterPro	IPR023346	Lysozyme-like domain superfamily
298	479	Gene3D	G3DSA:1.10.530.10	-
324	430	Pfam	PF01464	Transglycosylase SLT domain
324	430	InterPro	IPR008258	Transglycosylase SLT domain 1

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

0.873

Likely same site as FPocket 8 5.3 Å 27 shared residues 87% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.844

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Surrounding area

Pocket 3 P2Rank #3

0.044

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Surrounding area

Pocket 4 P2Rank #4

0.039

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Surrounding area

Pocket 5 P2Rank #5

0.025

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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

0.948 Unusual size

Likely same site as P2Rank 1 5.3 Å 27 shared residues 87% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:341-341

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.878

Likely same site as FPocket 1 4.5 Å 21 shared residues 72% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.737

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Surrounding area

Pocket 3 P2Rank #3

0.068

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Surrounding area

Pocket 4 P2Rank #4

0.045

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Surrounding area

Pocket 5 P2Rank #5

0.039

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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_A0A0H3GW83	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4617	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

6X4 PDB via homolog 489.6 Da · LogP -3.89 · TPSA 244.7 Open detail RCSB PDB

ZINC15722130 ZINC proposed compound · Tanimoto 0.582 Detail ZINC

ZINC255987061 ZINC proposed compound · Tanimoto 0.582 Detail ZINC

ZINC255987062 ZINC proposed compound · Tanimoto 0.582 Detail ZINC

ZINC255987063 ZINC proposed compound · Tanimoto 0.582 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
6X4 RCSB PDB	5AA4	A0A1I9GEN8	489.6 Da LogP -3.89 TPSA 244.7	1 viol.	✓ Clean	`C[C@H](C(=O)N)NC(=O)C(CCCC[NH3+])NC(=O)CC[C@H](…`

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
ZINC15722130 ZINC	0.582	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@@H](CCCCN)C(=O)…`
ZINC255987061 ZINC	0.582	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC255987062 ZINC	0.582	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC255987063 ZINC	0.582	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC255987064 ZINC	0.582	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC64219359 ZINC	0.565	202.3 Da LogP -0.41 TPSA 106.4	✓ Ro5	✓ Clean	`CC(C)[C@H](C(=O)[C@@H](C)N)[C@H](N)C(=O)O`
ZINC64219360 ZINC	0.565	202.3 Da LogP -0.41 TPSA 106.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](C(=O)[C@@H](C)N)[C@H](N)C(=O)O`
ZINC79670384 ZINC	0.565	202.3 Da LogP -0.41 TPSA 106.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](C(=O)[C@H](C)N)[C@H](N)C(=O)O`
ZINC79670387 ZINC	0.565	202.3 Da LogP -0.41 TPSA 106.4	✓ Ro5	✓ Clean	`CC(C)[C@H](C(=O)[C@H](C)N)[C@H](N)C(=O)O`
ZINC2516116 ZINC	0.559	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	0.559	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	0.559	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	0.559	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`
ZINC50027904 ZINC	0.559	261.3 Da LogP -1.51 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)C[C@H](N)C(=O)O)C(=O)O`
ZINC3055005 ZINC	0.556	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	0.556	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	0.556	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC100017163 ZINC	0.553	213.3 Da LogP 0.71 TPSA 99.2	✓ Ro5	✓ Clean	`C/C=C/CC(=N)NCCC[C@H](N)C(=O)O`
ZINC19796052 ZINC	0.553	219.2 Da LogP -1.73 TPSA 156.9	✓ Ro5	✓ Clean	`N/C(=N\[N+](=O)[O-])NCCC[C@H](N)C(=O)O`
ZINC21982226 ZINC	0.553	219.2 Da LogP -1.73 TPSA 156.9	✓ Ro5	✓ Clean	`N/C(=N\[N+](=O)[O-])NCCC[C@@H](N)C(=O)O`
ZINC5113209 ZINC	0.548	275.3 Da LogP -0.26 TPSA 138.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC13545298 ZINC	0.543	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCC(=O)NCCCC[C@H](N)C(=O)O`
ZINC6360447 ZINC	0.543	222.3 Da LogP 0.37 TPSA 75.3	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=S)S)C(=O)O`
ZINC5131766 ZINC	0.538	224.3 Da LogP -1.26 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)O`
ZINC1555366 ZINC	0.536	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	0.536	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	0.536	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	0.536	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	0.536	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	0.536	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC13529436 ZINC	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N1CCCCCC1`
ZINC19502834 ZINC	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)N1CCCCCC1`
ZINC19502836 ZINC	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](N)C(=O)N1CCCCCC1`
ZINC19502838 ZINC	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@H](N)C(=O)N1CCCCCC1`
ZINC1608689 ZINC	0.528	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCNC(=O)CC[C@H](N)C(=O)O`
ZINC1737889 ZINC	0.528	245.3 Da LogP -0.33 TPSA 118.4	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)NCCCC[C@H](N)C(=O)O`
ZINC1737892 ZINC	0.528	245.3 Da LogP -0.33 TPSA 118.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](N)C(=O)NCCCC[C@H](N)C(=O)O`
ZINC1737894 ZINC	0.528	245.3 Da LogP -0.33 TPSA 118.4	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)NCCCC[C@@H](N)C(=O)O`
ZINC1737898 ZINC	0.528	245.3 Da LogP -0.33 TPSA 118.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](N)C(=O)NCCCC[C@@H](N)C(=O)O`
ZINC2045835 ZINC	0.528	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCNC(=O)CC[C@@H](N)C(=O)O`
ZINC1529646 ZINC	0.526	290.3 Da LogP -1.78 TPSA 185.8	1 viol.	✓ Clean	`N=C(NCCC[C@H](N)C(=O)O)N[C@@H](CC(=O)O)C(=O)O`
ZINC2028776 ZINC	0.526	307.6 Da LogP 1.27 TPSA 101.6	✓ Ro5	✓ Clean	`N[C@@H](CCCNC(=O)OCC(Cl)(Cl)Cl)C(=O)O`
ZINC2028780 ZINC	0.526	307.6 Da LogP 1.27 TPSA 101.6	✓ Ro5	✓ Clean	`N[C@H](CCCNC(=O)OCC(Cl)(Cl)Cl)C(=O)O`
ZINC2043460 ZINC	0.526	214.3 Da LogP -0.52 TPSA 111.2	✓ Ro5	✓ Clean	`C=CCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC1848346 ZINC	0.520	216.3 Da LogP 0.20 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)N[C@H](C(=O)O)C(C)C`
ZINC1848348 ZINC	0.520	216.3 Da LogP 0.20 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)[C@H](N)C(C)C)C(=O)O`
ZINC1848350 ZINC	0.520	216.3 Da LogP 0.20 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)N[C@@H](C(=O)O)C(C)C`
ZINC1848352 ZINC	0.520	216.3 Da LogP 0.20 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](N)C(=O)N[C@@H](C(=O)O)C(C)C`
ZINC11959315 ZINC	0.516	213.3 Da LogP 0.13 TPSA 49.6	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N1CCN(C)CC1`
ZINC19504599 ZINC	0.516	213.3 Da LogP 0.13 TPSA 49.6	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](N)C(=O)N1CCN(C)CC1`

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 A0A0H3GW83