Protein target profile

VK055_0673

penicillin-binding protein 2

Genome: KpATCC43816 Gene: AIK79296.1 mrdA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GY10

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Length 636

Pocket druggability 0.074

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 60 total records

Functional annotation 1 EC 9 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Risks to review

Microbiome similarity 132 of 4744 screened genomes (2.8%) have a significant similarity hit. Mixed conservation Core/accessory calls are not fully concordant. Weak predicted binding pocket FPocket selected-pocket score 0.07.

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: 2.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 59.588 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 90.14 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.074

Structure A0A0H3GY10

Pocket Pocket 29

P2Rank 0.525

Structure A0A0H3GY10

Pocket Pocket 1

ColabFold model

FPocket 0.105 · Pocket 42

P2Rank 0.54 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 132 / 4744 genomes with a hit

Prevalence 2.8%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: no human homolog detected.

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MPLLRDEIRDHSAEEMLFIRRAAIAFLLVVVCFGVLIVNLYHLQVEQHDFYQTRSNQNDIKMLPIAPSRGLIFDRNGIPLVQNITLYRLQVIPSKIPDMAALLQQLTPIVDLTPDDIASFRDDMHHTSRYKAVTLKSDLSDVEVARFAVNEFRFPGVTVESYQQREYPYGAELAHVVGYVSKINDSDLQRLAKNGEEENYAADRNIGKQGIEGYYEKALHGTTGYQEVEVDNHGRVVRLLKEVPPVAGKNLYLTLDLHLQQYIESVLKGQRAAVVVVDPRDGGVLAMVSSPSYDPNPFVKGIGYQAYKSLLENPDRPLINRVTQGLYPPASTVKPYMALSALSAGVITPNTTFFGAPTWTLPGTQRRYRDWLKTGHGMLNVTKAIEESADTFFYQVAFEMGIDRIHEWLSKFGYGQSTGIDLNEEYAGVLPSREWKQRVHKKPWYQGDTISVGIGQGYWIATPIQMVKALTTLLNNGKVQDPHLLYSMKQGNHVERYQQPANLPQVGDPKSPYWGIVRNGMYGMANQPNGTGYKLFHTAPYQIAAKSGTSQVFSLKQNQTYNAKMIPVRLRDHIFYTLFAPYQHPKVAMALILENGGGDGVVAGPTARAILDHIFVPQQASSAAADVPQRDSADAQ

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

3.4.16.4

Gene Ontology (GO)

GO:0008658 Binding to penicillin, an antibiotic that contains the condensed beta-lactamthiazolidine ring system.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0009002 Catalysis of the reaction: (Ac)2-L-Lys-D-alanyl-D-alanine + H2O = (Ac)2-L-Lys-D-alanine + D-alanine.
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.
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:0071972 Catalysis of the reaction: 2 a peptidoglycan dimer (tetrapeptide) + 3 H2O = a peptidoglycan tetramer with L,D cross-links (L-Lys-D-Asn-L-Lys) + di-trans,poly-cis-undecaprenyl diphosphate + 4 D-alanine.
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:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0008360 Any process that modulates the surface configuration of a cell.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
4	619	Hamap	MF_02081	Peptidoglycan D,D-transpeptidase MrdA [mrdA].
4	619	InterPro	IPR017790	Penicillin-binding protein 2
273	612	Pfam	PF00905	Penicillin binding protein transpeptidase domain
273	612	InterPro	IPR001460	Penicillin-binding protein, transpeptidase
249	627	Gene3D	G3DSA:3.40.710.10	-
249	627	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
65	238	Pfam	PF03717	Penicillin-binding Protein dimerisation domain
65	238	InterPro	IPR005311	Penicillin-binding protein, dimerisation domain
65	248	Gene3D	G3DSA:3.90.1310.10	-
17	618	PANTHER	PTHR30627	PEPTIDOGLYCAN D,D-TRANSPEPTIDASE
249	623	FunFam	G3DSA:3.40.710.10:FF:000004	Peptidoglycan D,D-transpeptidase MrdA
58	254	SUPERFAMILY	SSF56519	Penicillin binding protein dimerisation domain
58	254	InterPro	IPR036138	Penicillin-binding protein, dimerisation domain superfamily
255	615	SUPERFAMILY	SSF56601	beta-lactamase/transpeptidase-like
255	615	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
21	43	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
21	43	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
44	636	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
86	161	Gene3D	G3DSA:3.30.1390.30	-
1	20	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
155	249	FunFam	G3DSA:3.90.1310.10:FF:000001	Peptidoglycan D,D-transpeptidase MrdA
20	615	NCBIfam	TIGR03423	penicillin-binding protein 2
20	615	InterPro	IPR017790	Penicillin-binding protein 2

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

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.525

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Surrounding area

Site 2 P2Rank #2

0.221

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Surrounding area

Site 3 P2Rank #3

0.086

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Surrounding area

Site 4 P2Rank #4

0.059

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Surrounding area

Site 5 P2Rank #5

0.029

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Surrounding area

Residue sets

UniProt: Active site:316-316 Acyl-ester intermediate

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.54

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Surrounding area

Site 2 P2Rank #2

0.11

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Surrounding area

Site 3 P2Rank #3

0.065

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Surrounding area

Site 4 P2Rank #4

0.017

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Surrounding area

Site 5 P2Rank #5

0.017

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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_A0A0H3GY10	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0673	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 and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 6 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ET5 PDB via homolog 334.3 Da · LogP -0.93 · TPSA 168.2 Open detail RCSB PDB

JPP PDB via homolog Detail RCSB PDB

NXL PDB via homolog Detail RCSB PDB

RB6 PDB via homolog Detail RCSB PDB

CHEMBL4560540 ChEMBL via homolog · pchembl 8.00 (~10.0 nM) Detail ChEMBL

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
ET5 RCSB PDB	6G9S	P0AD65	334.3 Da LogP -0.93 TPSA 168.2	✓ Ro5	✓ Clean	`c1c(ocn1)C2=C[C@H](N(C[C@@H]2NOS(=O)(=O)O)C(=O)…`
JPP RCSB PDB	6H5O	A0A0H3JPA5	519.6 Da LogP -0.29 TPSA 165.2	1 viol.	✓ Clean	`CCN1CCN(C(=O)C1=O)C(=O)N[C@H](c2ccccc2)C(=O)N[C…`
NXL RCSB PDB	6G9F	P0AD65	267.3 Da LogP -2.21 TPSA 139.0	✓ Ro5	✓ Clean	`C1C[C@H](N(C[C@@H]1NOS(=O)(=O)O)C=O)C(=O)N`
RB6 RCSB PDB	6G88	Q47759	536.6 Da LogP -1.50 TPSA 212.2	3 viol.	✓ Clean	`C1CNC[C@@H]1N2CC=C(C2=O)CC3=C(N[C@H](SC3)[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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL4560540 ChEMBL	P0AD65	8.00 ~10.0 nM	316.3 Da LogP -0.76 TPSA 139.2	✓ Ro5	✓ Clean	`NC[C@@H]1C=C(c2cnco2)[C@@H]2CN1C(=O)N2OS(=O)(=O…`
CHEMBL2107817 ChEMBL	P0AD65	6.23 ~588.8 nM	287.2 Da LogP -4.86 TPSA 133.1	✓ Ro5	✓ Clean	`NC(=O)[C@@H]1CC[C@@H]2CN1C(=O)N2OS(=O)(=O)[O-].…`
CHEMBL1359 ChEMBL	Q2TL65	—	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
CHEMBL520642 ChEMBL	Q7DHH4	—	534.6 Da LogP -1.44 TPSA 203.4	2 viol.	✓ Clean	`Nc1nc(/C(=N/O)C(=O)N[C@@H]2C(=O)N3C(C(=O)O)=C(/…`
CHEMBL530 ChEMBL	P0AD65	—	325.4 Da LogP 1.41 TPSA 73.2	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](/N=C/N3CCCCCC3)C(=O)N2[C@H]…`
CHEMBL819 ChEMBL	Q7DHH4	—	401.4 Da LogP 1.90 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2)c1C(=O)N[C@@H]1C(=O)N2[C@@H]1S…`

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
ZINC1536458 ZINC	1.000	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@@H]1C(S[C@H]2CN[C@@H](C(=O)Nc3cccc(C(=O)O)c…`
ZINC216618654 ZINC	1.000	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC242543275 ZINC	1.000	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@@H]1C(S[C@@H]2CN[C@H](C(=O)Nc3cccc(C(=O)O)c…`
ZINC242543276 ZINC	1.000	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC242543277 ZINC	1.000	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC3831241 ZINC	1.000	401.4 Da LogP 1.90 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2)c1C(=O)N[C@@H]1C(=O)N2[C@@H]1S…`
ZINC3831242 ZINC	1.000	401.4 Da LogP 1.90 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2)c1C(=O)N[C@H]1C(=O)N2[C@H]1SC(…`
ZINC3831243 ZINC	1.000	401.4 Da LogP 1.90 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2)c1C(=O)N[C@@H]1C(=O)N2[C@H]1SC…`
ZINC3875439 ZINC	1.000	401.4 Da LogP 1.90 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2)c1C(=O)N[C@@H]1C(=O)N2[C@@H](C…`
ZINC3918453 ZINC	1.000	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC43769660 ZINC	1.000	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@H]1C(S[C@H]2CN[C@@H](C(=O)Nc3cccc(C(=O)O)c3…`
ZINC43769661 ZINC	1.000	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@H]3CN[C…`
ZINC43769662 ZINC	1.000	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@@H]1C(S[C@H]2CN[C@@H](C(=O)Nc3cccc(C(=O)O)c…`
ZINC9212279 ZINC	1.000	401.4 Da LogP 1.90 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2)c1C(=O)N[C@@H]1C(=O)N2[C@H]1SC…`
ZINC95486481 ZINC	1.000	475.5 Da LogP 0.94 TPSA 156.3	✓ Ro5	✓ Clean	`C[C@H]1C(S[C@@H]2CN[C@H](C(=O)Nc3cccc(C(=O)O)c3…`
ZINC1551650 ZINC	0.816	265.2 Da LogP -1.53 TPSA 130.2	✓ Ro5	✓ Clean	`NC(=O)[C@H]1CC[C@H]2CN1C(=O)N2OS(=O)(=O)O`
ZINC33979726 ZINC	0.816	265.2 Da LogP -1.53 TPSA 130.2	✓ Ro5	✓ Clean	`NC(=O)[C@H]1CC[C@@H]2CN1C(=O)N2OS(=O)(=O)O`
ZINC3966153 ZINC	0.816	265.2 Da LogP -1.53 TPSA 130.2	✓ Ro5	✓ Clean	`NC(=O)[C@@H]1CC[C@H]2CN1C(=O)N2OS(=O)(=O)O`
ZINC9302239 ZINC	0.816	265.2 Da LogP -1.53 TPSA 130.2	✓ Ro5	✓ Clean	`NC(=O)[C@@H]1CC[C@@H]2CN1C(=O)N2OS(=O)(=O)O`
ZINC21986197 ZINC	0.790	435.9 Da LogP 2.55 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C@H]1…`
ZINC3830593 ZINC	0.790	435.9 Da LogP 2.55 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C@@H]…`
ZINC3830594 ZINC	0.790	435.9 Da LogP 2.55 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2Cl)c1C(=O)N[C@H]1C(=O)N2[C@H]1S…`
ZINC3830595 ZINC	0.790	435.9 Da LogP 2.55 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C@H]1…`
ZINC3875417 ZINC	0.790	435.9 Da LogP 2.55 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2ccccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C@@H]…`
ZINC1530612 ZINC	0.787	470.3 Da LogP 3.20 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(Cl)cccc2Cl)c1C(=O)N[C@H]1C(=O)N2[C@…`
ZINC2015281 ZINC	0.787	470.3 Da LogP 3.20 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(Cl)cccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C…`
ZINC3830690 ZINC	0.787	470.3 Da LogP 3.20 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(Cl)cccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C…`
ZINC3830691 ZINC	0.787	470.3 Da LogP 3.20 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(Cl)cccc2Cl)c1C(=O)N[C@H]1C(=O)N2[C@…`
ZINC3830692 ZINC	0.787	470.3 Da LogP 3.20 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(Cl)cccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C…`
ZINC3978006 ZINC	0.787	470.3 Da LogP 3.20 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(Cl)cccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C…`
ZINC1532344 ZINC	0.750	453.9 Da LogP 2.69 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(F)cccc2Cl)c1C(=O)N[C@H]1C(=O)N2[C@@…`
ZINC3830843 ZINC	0.750	453.9 Da LogP 2.69 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(F)cccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C@…`
ZINC3830844 ZINC	0.750	453.9 Da LogP 2.69 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(F)cccc2Cl)c1C(=O)N[C@H]1C(=O)N2[C@H…`
ZINC3830845 ZINC	0.750	453.9 Da LogP 2.69 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(F)cccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C@…`
ZINC4102187 ZINC	0.750	453.9 Da LogP 2.69 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(F)cccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C@…`
ZINC9230633 ZINC	0.750	453.9 Da LogP 2.69 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1onc(-c2c(F)cccc2Cl)c1C(=O)N[C@@H]1C(=O)N2[C@…`
ZINC5159702 ZINC	0.698	381.5 Da LogP 1.45 TPSA 79.3	✓ Ro5	✓ Clean	`CC(=O)COC(=O)[C@@H]1N2C(=O)[C@@H](/N=C/N3CCCCCC…`
ZINC21984184 ZINC	0.652	383.5 Da LogP -0.31 TPSA 110.2	✓ Ro5	✓ Clean	`C[C@@H]1C(S[C@@H]2CN[C@H](C(=O)N(C)C)C2)=C(C(=O…`
ZINC245204572 ZINC	0.652	383.5 Da LogP -0.31 TPSA 110.2	✓ Ro5	✓ Clean	`C[C@@H]1C(S[C@@H]2CN[C@H](C(=O)N(C)C)C2)=C(C(=O…`
ZINC245204573 ZINC	0.652	383.5 Da LogP -0.31 TPSA 110.2	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC28636621 ZINC	0.652	383.5 Da LogP -0.31 TPSA 110.2	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC3808779 ZINC	0.652	383.5 Da LogP -0.31 TPSA 110.2	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC44672480 ZINC	0.652	383.5 Da LogP -0.31 TPSA 110.2	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC44675971 ZINC	0.652	383.5 Da LogP -0.31 TPSA 110.2	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[…`
ZINC5736072 ZINC	0.652	383.5 Da LogP -0.31 TPSA 110.2	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC5736130 ZINC	0.652	383.5 Da LogP -0.31 TPSA 110.2	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC95486475 ZINC	0.652	383.5 Da LogP -0.31 TPSA 110.2	✓ Ro5	✓ Clean	`C[C@H]1C(S[C@@H]2CN[C@H](C(=O)N(C)C)C2)=C(C(=O)…`
ZINC11616332 ZINC	0.649	439.6 Da LogP 2.41 TPSA 88.5	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)OCOC(=O)[C@@H]1N2C(=O)[C@H](N=CN3C…`
ZINC2010430 ZINC	0.649	439.6 Da LogP 2.41 TPSA 88.5	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)OCOC(=O)[C@@H]1N2C(=O)[C@H](/N=C/N…`
ZINC3874699 ZINC	0.649	439.6 Da LogP 2.41 TPSA 88.5	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)OCOC(=O)[C@@H]1N2C(=O)[C@@H](/N=C/…`

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.

VK055_0673

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Chemistry

Pathways

Metabolic context

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · P2Rank

Structural evidence

Ligand evidence