Protein target profile

VK055_1865

penicillin-binding protein 2

Genome: KpATCC43816 Gene: mrdA2 AIK80471.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GTX1

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Length 633

Pocket druggability 0.315

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 79 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 0.72. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Microbiome similarity 146 of 4744 screened genomes (3.1%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.32.

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: 3.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 93.207 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: 90.4 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 0.315

Structure A0A0H3GTX1

Pocket Pocket 7

P2Rank 0.724

Structure A0A0H3GTX1

Pocket Pocket 1

ColabFold model

FPocket 0.11 · Pocket 14

P2Rank 0.932 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 146 / 4744 genomes with a hit

Prevalence 3.1%

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.

MKLQNSFRDYTAESSLFVRRALVAFLGILLLTGVLIANLYNVQIVRFDDYQTRSNENRIKLVPIPPSRGIIYDRNGTPLALNRTIYQLEMMPEKVDNVQQTLDALRDVVDLTDDDIAGFKKERARSHRFTSIPVKVNLSEVQVARFAVNQYRFPGVEVKGYKRRYYPYNSALTHVIGYVSKINDKDVDRLDKEGKLANYASTHDIGKLGIERYYEDVLHGQTGYEEVEVNNRGRVIRQLKEVPPQAGRDIYLTLDLKLQQYIETLLAGSRAAVVVTDPRTGAILALVSTPSYDPNLFVDGISSKDYSALLNDPNTPLVNRATQGVYPPASTVKPYVAVSALSAGVITRNTSLFDPGWWQLPGSEKRYRDWKKWGHGHLNVTKALEESADTYFYQVAYDMGIDRLSEWMSKFGYGHYTGIDLSEERSGNMPTREWKLKRFKKPWYQGDTIPVGIGQGYWTATPIQMNKALMILINDGVVKVPHLLQSTVEDGKPVPWVQPHEPPVGDIHSGYWEIAKDGMYGVANRGNGTAHKYFASAPYKIAAKSGTAQVFGLKANETYNAHRISERLRDHKLMTAFAPYNNPQVAVAMILENGGAGPAVGTIMRQILDHIMLGDNNTTLPSENPAVTAGEDQ

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.

24 records

Show feature table

Start	End	DB	Term	Name
85	160	Gene3D	G3DSA:3.30.1390.30	-
19	612	NCBIfam	TIGR03423	penicillin-binding protein 2
19	612	InterPro	IPR017790	Penicillin-binding protein 2
248	620	FunFam	G3DSA:3.40.710.10:FF:000004	Peptidoglycan D,D-transpeptidase MrdA
64	239	Pfam	PF03717	Penicillin-binding Protein dimerisation domain
64	239	InterPro	IPR005311	Penicillin-binding protein, dimerisation domain
21	40	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
254	611	SUPERFAMILY	SSF56601	beta-lactamase/transpeptidase-like
254	611	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
21	43	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
85	160	FunFam	G3DSA:3.30.1390.30:FF:000001	Peptidoglycan D,D-transpeptidase MrdA
64	248	Gene3D	G3DSA:3.90.1310.10	-
1	20	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
15	619	PANTHER	PTHR30627	PEPTIDOGLYCAN D,D-TRANSPEPTIDASE
56	253	SUPERFAMILY	SSF56519	Penicillin binding protein dimerisation domain
56	253	InterPro	IPR036138	Penicillin-binding protein, dimerisation domain superfamily
3	616	Hamap	MF_02081	Peptidoglycan D,D-transpeptidase MrdA [mrdA].
3	616	InterPro	IPR017790	Penicillin-binding protein 2
272	609	Pfam	PF00905	Penicillin binding protein transpeptidase domain
272	609	InterPro	IPR001460	Penicillin-binding protein, transpeptidase
41	633	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
152	248	FunFam	G3DSA:3.90.1310.10:FF:000001	Peptidoglycan D,D-transpeptidase MrdA
249	619	Gene3D	G3DSA:3.40.710.10	-
249	619	InterPro	IPR012338	Beta-lactamase/transpeptidase-like

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 · FPocket

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

Site 1 FPocket #7

0.315

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Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.724

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Surrounding area

Site 2 P2Rank #2

0.094

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Surrounding area

Site 3 P2Rank #3

0.091

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Surrounding area

Site 4 P2Rank #4

0.022

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Surrounding area

Site 5 P2Rank #5

0.018

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Surrounding area

Residue sets

UniProt: Active site:330-330 Acyl-ester intermediate

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.932

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Surrounding area

Site 2 P2Rank #2

0.144

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Surrounding area

Site 3 P2Rank #3

0.016

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Surrounding area

Site 4 P2Rank #4

0.016

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Surrounding area

Site 5 P2Rank #5

0.015

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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_A0A0H3GTX1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1865	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.

79 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 29 records from similar proteins

Structural ligands 25 0 loaded crystals

Measured bioactivity 4 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0W0 PDB via homolog 672.6 Da · LogP -2.06 · TPSA 328.0 Open detail RCSB PDB

59F PDB via homolog Detail RCSB PDB

59H PDB via homolog Detail RCSB PDB

59J PDB via homolog Detail RCSB PDB

AI8 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
0W0 RCSB PDB	4FSF	Q51504	672.6 Da LogP -2.06 TPSA 328.0	3 viol.	✓ Clean	`CC(C)(C(=O)O)O/N=C(/c1csc(n1)N)\C(=O)N[C@H](C=O…`
59F RCSB PDB	5DF8	Q51504	535.6 Da LogP -0.73 TPSA 185.4	1 viol.	✓ Clean	`CCN1CCN(C(=O)C1=O)C(=O)N[C@H](c2ccc(cc2)O)C(=O)…`
59H RCSB PDB	5DF7	Q51504	463.5 Da LogP 0.04 TPSA 156.9	✓ Ro5	✓ Clean	`CC1([C@@H](N[C@H](S1)[C@@H](C=O)NC(=O)[C@@H](c2…`
59J RCSB PDB	5DF9	Q51504	549.6 Da LogP -0.36 TPSA 206.0	1 viol.	✓ Clean	`CCN1CCN(C(=O)C1=O)C(=O)N[C@H](c2ccc(cc2)O)C(=O)…`
AI8 RCSB PDB	6MKI	Q9K3C9	607.7 Da LogP 1.24 TPSA 185.7	2 viol.	✓ Clean	`CCON=C(c1nc(sn1)N)C(=O)N[C@H](C=O)[C@@H]2NC(=C(…`
AXL RCSB PDB	6I1E	G3XD46	367.4 Da LogP -0.03 TPSA 141.8	✓ Ro5	✓ Clean	`CC1([C@@H](N[C@H](S1)[C@@H](C=O)NC(=O)[C@@H](c2…`
AZR RCSB PDB	3PBS	Q51504	437.5 Da LogP -1.23 TPSA 210.4	✓ Ro5	✓ Clean	`C[C@@H]([C@@H](C=O)NC(=O)/C(=N\OC(C)(C)C(=O)O)/…`
CAZ RCSB PDB	3PBO	G3XD46	469.5 Da LogP 0.15 TPSA 193.6	1 viol.	✓ Clean	`CC(C)(C(=O)O)O/N=C(/c1csc(n1)N)\C(=O)N[C@H](C=O…`
CB9 RCSB PDB	3OCL	Q51504	380.4 Da LogP 0.43 TPSA 132.8	✓ Ro5	✓ Clean	`CC1([C@@H](N[C@H](S1)[C@@H](C=O)NC(=O)[C@H](c2c…`
CTJ RCSB PDB	3OCN	Q51504	549.6 Da LogP -0.02 TPSA 197.2	2 viol.	✓ Clean	`CC(C)(C(=O)O)O/N=C(/c1csc(n1)N)\C(=O)N[C@H](C=O…`
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)…`
IM2 RCSB PDB	6MKF	A0A075Q0W3	301.4 Da LogP -0.23 TPSA 122.5	✓ Ro5	✓ Clean	`[H]/N=C/NCCSC1=C(N[C@H](C1)[C@H](C=O)[C@@H](C)O…`
JPP RCSB PDB	4KQO	G3XD46	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…`
MER RCSB PDB	3PBR	G3XD46	385.5 Da LogP -0.36 TPSA 119.0	✓ Ro5	✓ Clean	`C[C@@H]1[C@@H](NC(=C1S[C@H]2C[C@H](NC2)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`
ODZ RCSB PDB	6Y6U	G3XD46	263.3 Da LogP 1.47 TPSA 86.6	✓ Ro5	✓ Clean	`C[C@](CC(=C)O)(C=O)NC(=O)Cc1ccc(cc1)O`
OEE RCSB PDB	6Y6Z	G3XD46	229.3 Da LogP 1.93 TPSA 75.6	✓ Ro5	✓ Clean	`C[C@](CC(=C)O)(C=O)NC(=O)OC(C)(C)C`
PFV RCSB PDB	4L0L	Q51504	634.6 Da LogP -2.64 TPSA 314.0	3 viol.	✓ Clean	`CC(C)(C(=O)O)O/N=C(/c1csc(n1)N)\C(=O)N[C@H](C=O…`
PNM RCSB PDB	6MKG	A0A075Q0W3	336.4 Da LogP 0.81 TPSA 95.5	✓ Ro5	✓ Clean	`CC1([C@@H](N[C@H](S1)[C@@H](C=O)NC(=O)Cc2ccccc2…`
R7G RCSB PDB	6VOT	G3XD46	688.6 Da LogP -2.02 TPSA 303.5	3 viol.	Alert	`CC(C)(C(=O)O)O/N=C(/c1csc(n1)N)\C(=O)N[C@@H](CN…`
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]…`
TJ7 RCSB PDB	6UN1	G3XD46	416.5 Da LogP 0.47 TPSA 142.0	✓ Ro5	✓ Clean	`CC1([C@@H](N[C@H](S1)[C@@](C=O)(NC(=O)[C@@H](c2…`
UE1 RCSB PDB	3PBT	G3XD46	715.7 Da LogP -5.06 TPSA 355.7	3 viol.	✓ Clean	`CC(C)(C(=O)[O-])O/N=C(/c1csc(n1)N)\C(=O)N[C@@H]…`
VPP RCSB PDB	4KQQ	G3XD46	535.6 Da LogP -0.41 TPSA 185.4	1 viol.	✓ Clean	`CCN1CCN(C(=O)C1=O)C(=O)N[C@H](c2ccccc2)C(=O)N[C…`
XT8 RCSB PDB	6UN3	G3XD46	386.5 Da LogP 0.49 TPSA 132.8	✓ Ro5	✓ Clean	`CC1([C@@H](N[C@H](S1)[C@@H](C=O)NC(=O)[C@@H](c2…`

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…`
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]…`

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
ZINC11677186 ZINC	1.000	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@@…`
ZINC12469558 ZINC	1.000	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]…`
ZINC13828187 ZINC	1.000	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…`
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…`
ZINC1857573562 ZINC	1.000	325.4 Da LogP 1.41 TPSA 73.2	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](N=CN3CCCCCC3)C(=O)N2[C@H]1C…`
ZINC2010421 ZINC	1.000	325.4 Da LogP 1.41 TPSA 73.2	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@@H](N=CN3CCCCCC3)C(=O)N2[C@@H]…`
ZINC2053528119 ZINC	1.000	325.4 Da LogP 1.41 TPSA 73.2	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@@H](N=CN3CCCCCC3)C(=O)N2[C@H]1…`
ZINC2053528120 ZINC	1.000	325.4 Da LogP 1.41 TPSA 73.2	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](N=CN3CCCCCC3)C(=O)N2[C@@H]1…`
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…`
ZINC3830206 ZINC	1.000	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]…`
ZINC3830207 ZINC	1.000	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…`
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…`
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`
ZINC13520637 ZINC	0.720	352.4 Da LogP 0.69 TPSA 115.7	✓ Ro5	✓ Clean	`CC1(C)S[C@H]([C@@H](NC(=O)Cc2ccccc2)C(=O)O)N[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…`
ZINC11616333 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…`
ZINC13704173 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\…`
ZINC1857622099 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=CN3…`
ZINC1903864089 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=CN3…`
ZINC1903864090 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/…`
ZINC4214799 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/…`
ZINC72481794 ZINC	0.611	229.3 Da LogP 1.93 TPSA 75.6	✓ Ro5	✓ Clean	`C=C[C@](C)(CC(=O)O)NC(=O)OC(C)(C)C`
ZINC72481795 ZINC	0.611	229.3 Da LogP 1.93 TPSA 75.6	✓ Ro5	✓ Clean	`C=C[C@@](C)(CC(=O)O)NC(=O)OC(C)(C)C`
ZINC2569283 ZINC	0.609	335.3 Da LogP -0.08 TPSA 127.2	✓ Ro5	✓ Clean	`CCN1CCN(C(=O)N[C@@H](C(=O)O)c2ccc(O)cc2)C(=O)C1…`
ZINC4556304 ZINC	0.609	335.3 Da LogP -0.08 TPSA 127.2	✓ Ro5	✓ Clean	`CCN1CCN(C(=O)N[C@H](C(=O)O)c2ccc(O)cc2)C(=O)C1=O`
ZINC255982699 ZINC	0.589	367.4 Da LogP 0.15 TPSA 141.8	✓ Ro5	✓ Clean	`CC1(C)S[C@H]([C@H](NC(=O)[C@@H](N)c2ccccc2)C(=O…`
ZINC34648375 ZINC	0.589	367.4 Da LogP 0.15 TPSA 141.8	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]([C@@H](NC(=O)[C@H](N)c2ccccc2)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_1865

Promising target candidate with multiple supporting evidence streams.

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 · FPocket

Binding pockets · P2Rank

Binding pockets · P2Rank

Structural evidence

Ligand evidence