Protein target profile

KP13_00697

Penicillin-binding protein 1A

Genome: KpKP13 Gene: mrcA AHE42316.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GZF1

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Length 852

Pocket druggability 0.568

Direct ligand evidence 0 68 total records

Functional annotation 2 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

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

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: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 42.208 Higher values support similarity to known essential genes.
DEG E-value: 9.44e-151 Smaller values mean stronger essential-gene similarity.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 89.95 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 0.568

Structure A0A0H3GZF1

Pocket Pocket 5

P2Rank 0.566

Structure A0A0H3GZF1

Pocket Pocket 1

ColabFold model

FPocket 0.574 · Pocket 42

P2Rank 0.526 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 140 / 4744 genomes with a hit

Prevalence 3.0%

Cross-references

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

Sequence

UniProt A0A0H3GZF1

Chemistry

ChEMBL CHEMBL3265226 ChEMBL CHEMBL3265220 ChEMBL CHEMBL3265221 ChEMBL CHEMBL3265224 ChEMBL CHEMBL3265225 ChEMBL CHEMBL3265223 ChEMBL CHEMBL3265222

Sequence

Primary amino-acid sequence viewer.

MKFVKYLLILAVCCVLLGAGSIFGLYKYIEPQLPDVATLKDVRLQIPMQVYSADGELIAQYGEKRRIPVTLQQIPPELVKAFIATEDSRFYEHHGVDPVGIFRAASVAMFSGHASQGASTITQQLARNFFLSPEKTLMRKIKEAFLAIRIEQLLNKDEILELYLNKIYLGYRAYGVGAAAQVYFGKPIDQLTLSEMAVIAGLPKAPSTFNPLYSMDRATARRNVVLSRMLSEGYITQAQYDEARSEPIDASYHAPKIAFSAPYLSEMVRQEMVNRYGEQAYEDGYRVYTTITRKNQQAAQQAVRNNVLDYDMRHGYRGPASVLWKVGETPWETKKIVDSLKRQSGYGPLFPAVVTSANAQEAVALLANGDSVSLTMEGVRWARRFISDTQQGATPRKVNDVVQAGQQIWVRKVGDSWWLSQLPDVNSALVSINPQNGAIIALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGLTLASMLNDVPISRWDAGAGSDWRPKNSPPQYAGPIRLRQGLGQSKNVVMVRAMRAMGVDYAAEYLQRFGFPAQNIVHTESLALGSASFTPLQVARGYSVMANGGFLVNPFFISKIENDQGGVLFEERPKIACPQCDLPVIYGDTPKSNVLENKDVEDVATSAEPQNGNVPPQPQLEQANQSLVAQSGAQEYAPHVINTPLAFLIKSALNSNIFGEPGWMGTGWRAGRDLQRHDIGGKTGTTNSSKDAWFSGYGPGVVTSVWIGFDDHRRDLGRTTASGAIKDQISGYEGGAKSAQPAWDSFMKSVLEGVPEEPLTPPPGIVTVNIDRSTGQLANGGNSRAEYFIEGTQPTQQAVREVGTTLTDGGGETHELF

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 10 GO

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0008658 Binding to penicillin, an antibiotic that contains the condensed beta-lactamthiazolidine ring system.
GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
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: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:0009002 Catalysis of the reaction: (Ac)2-L-Lys-D-alanyl-D-alanine + H2O = (Ac)2-L-Lys-D-alanine + 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: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: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.
GO:0046677 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
55	229	Pfam	PF00912	Transglycosylase
55	229	InterPro	IPR001264	Glycosyl transferase, family 51
25	852	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
243	326	Gene3D	G3DSA:3.40.710.10	-
243	326	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
48	242	Gene3D	G3DSA:1.10.3810.10	-
48	242	InterPro	IPR036950	Penicillin binding protein transglycosylase domain
243	332	FunFam	G3DSA:3.40.710.10:FF:000013	Penicillin-binding protein 1A
43	257	SUPERFAMILY	SSF53955	Lysozyme-like
43	257	InterPro	IPR023346	Lysozyme-like domain superfamily
397	834	FunFam	G3DSA:3.40.710.10:FF:000010	Penicillin-binding protein 1A
65	786	NCBIfam	TIGR02074	PBP1A family penicillin-binding protein
2	837	PANTHER	PTHR32282	BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED
1	6	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
7	29	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
395	834	Gene3D	G3DSA:3.40.710.10	-
395	834	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
429	603	Pfam	PF00905	Penicillin binding protein transpeptidase domain
429	603	InterPro	IPR001460	Penicillin-binding protein, transpeptidase
1	24	Phobius	SIGNAL_PEPTIDE	Signal peptide region
18	24	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
211	832	SUPERFAMILY	SSF56601	beta-lactamase/transpeptidase-like
211	832	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
7	17	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
48	242	FunFam	G3DSA:1.10.3810.10:FF:000003	Penicillin-binding protein 1a
316	425	Pfam	PF17092	Penicillin-binding protein OB-like domain
316	425	InterPro	IPR031376	Penicillin-binding protein, OB-like domain

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 #5

0.568

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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

0.566

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Surrounding area

Site 2 P2Rank #2

0.311

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Surrounding area

Site 3 P2Rank #3

0.08

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Surrounding area

Site 4 P2Rank #4

0.062

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Surrounding area

Site 5 P2Rank #5

0.011

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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

0.526

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Surrounding area

Site 2 P2Rank #2

0.278

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Surrounding area

Site 3 P2Rank #3

0.079

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Surrounding area

Site 4 P2Rank #4

0.063

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Surrounding area

Site 5 P2Rank #5

0.058

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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_A0A0H3GZF1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00697	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.

68 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 18 records from similar proteins

Structural ligands 11 0 loaded crystals

Measured bioactivity 7 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2U4 PDB via homolog 664.6 Da · LogP -1.00 · TPSA 318.0 Open detail RCSB PDB

AZR PDB via homolog Detail RCSB PDB

BMG PDB via homolog Detail RCSB PDB

CB9 PDB via homolog Detail RCSB PDB

DXF 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
2U4 RCSB PDB	4OON	Q07806	664.6 Da LogP -1.00 TPSA 318.0	3 viol.	Alert	`CC(C)(C(=O)O)O/N=C(/c1csc(n1)N)\C(=O)N[C@@H](CO…`
AZR RCSB PDB	3UE0	G1C794	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)/…`
BMG RCSB PDB	2ZC5	Q04707	352.4 Da LogP -1.95 TPSA 111.2	✓ Ro5	✓ Clean	`C[C@@H]1[C@@H](NC(=C1S[C@@H]2Cn3cnc[n+]3C2)C(=O…`
CB9 RCSB PDB	3ZGA	Q8Y547	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…`
DXF RCSB PDB	3ZG9	Q8Y547	426.4 Da LogP -0.59 TPSA 182.6	✓ Ro5	✓ Clean	`CO/N=C(/c1ccco1)\C(=O)N[C@H](C=O)[C@@H]2NC(=C(C…`
IM2 RCSB PDB	3UDX	G1C794	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…`
M0E RCSB PDB	2OLV	Q9R744	1580.6 Da LogP -2.25 TPSA 607.7	3 viol.	✓ Clean	`C[C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O[C@@H]2[C…`
PNM RCSB PDB	3UDI	G1C794	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…`
TEB RCSB PDB	2ZC6	Q04707	385.5 Da LogP 0.61 TPSA 102.2	✓ Ro5	✓ Clean	`C[C@@H]1[C@@H](NC(=C1SC2CN(C2)C3=NCCS3)C(=O)O)[…`
TLA RCSB PDB	3ZG7	Q8Y547	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=O)O)O`
UE1 RCSB PDB	3UE1	G1C794	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]…`

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
CHEMBL3265226 ChEMBL	Q07806	7.52 ~30.2 nM	662.5 Da LogP -1.63 TPSA 297.9	3 viol.	Alert	`CC(C)(O/N=C(\C(=O)N[C@H]1CON(C2(C(=O)O)C[C@H](N…`
CHEMBL3265220 ChEMBL	Q07806	7.34 ~45.7 nM	485.4 Da LogP -1.31 TPSA 220.0	1 viol.	✓ Clean	`CC(C)(O/N=C(\C(=O)N[C@H]1CON(C2(C(=O)O)CCC(=O)O…`
CHEMBL3265221 ChEMBL	Q07806	7.34 ~45.7 nM	538.5 Da LogP -1.87 TPSA 245.2	2 viol.	✓ Clean	`Nc1nc(/C(=N/OCc2cc(=O)c(O)cn2O)C(=O)N[C@H]2CON(…`
CHEMBL3265224 ChEMBL	Q07806	7.34 ~45.7 nM	653.5 Da LogP -2.80 TPSA 311.6	3 viol.	✓ Clean	`CC(C)(O/N=C(\C(=O)N[C@H]1CON(C2(C(=O)O)C[C@@H](…`
CHEMBL3265225 ChEMBL	Q07806	7.34 ~45.7 nM	653.5 Da LogP -2.80 TPSA 311.6	3 viol.	✓ Clean	`CC(C)(O/N=C(\C(=O)N[C@H]1CON(C2(C(=O)O)C[C@H](N…`
CHEMBL3265223 ChEMBL	Q07806	7.19 ~64.6 nM	634.6 Da LogP -0.41 TPSA 258.4	2 viol.	✓ Clean	`CC(C)(O/N=C(\C(=O)N[C@H]1CON(C2(C(=O)O)C[C@H](N…`
CHEMBL3265222 ChEMBL	Q07806	6.96 ~109.6 nM	634.6 Da LogP -0.41 TPSA 258.4	2 viol.	✓ Clean	`CC(C)(O/N=C(\C(=O)N[C@H]1CON(C2(C(=O)O)C[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
ZINC4576926 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@…`
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)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…`
ZINC255982700 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…`
ZINC34064296 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…`
ZINC34064298 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)…`
ZINC34064299 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(=…`
ZINC34648377 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…`
ZINC1560405156 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC15848211 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@@H]1[C@H](NC(=O)/C(=N\OC(C)(C)C(=O)O)c2csc(…`
ZINC16958002 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@H]1[C@@H](NC(=O)/C(=N/OC(C)(C)C(=O)O)c2csc(…`
ZINC17214369 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@@H]1[C@@H](NC(=O)/C(=N/OC(C)(C)C(=O)O)c2csc…`
ZINC252430978 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@H]1[C@H](NC(=O)C(=NOC(C)(C)C(=O)O)c2csc(N)n…`
ZINC256010240 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@H]1[C@@H](NC(=O)C(=NOC(C)(C)C(=O)O)c2csc(N)…`
ZINC256010241 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@@H]1[C@@H](NC(=O)C(=NOC(C)(C)C(=O)O)c2csc(N…`
ZINC256010242 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@@H]1[C@H](NC(=O)C(=NOC(C)(C)C(=O)O)c2csc(N)…`
ZINC3830263 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@@H]1[C@H](NC(=O)/C(=N/OC(C)(C)C(=O)O)c2csc(…`
ZINC3830264 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@H]1[C@H](NC(=O)/C(=N\OC(C)(C)C(=O)O)c2csc(N…`
ZINC3830266 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@H]1[C@@H](NC(=O)/C(=N\OC(C)(C)C(=O)O)c2csc(…`
ZINC4676362 ZINC	0.564	435.4 Da LogP -1.17 TPSA 201.6	✓ Ro5	✓ Clean	`C[C@@H]1[C@@H](NC(=O)/C(=N\OC(C)(C)C(=O)O)c2csc…`
ZINC254005599 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CON=C(C(=O)N[C@@H]1C(=O)N2C(C(=O)O)=C(COC(N)=O)…`
ZINC271775151 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CON=C(C(=O)N[C@H]1C(=O)N2C(C(=O)O)=C(COC(N)=O)C…`
ZINC271775157 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CON=C(C(=O)N[C@H]1C(=O)N2C(C(=O)O)=C(COC(N)=O)C…`
ZINC271775161 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CON=C(C(=O)N[C@@H]1C(=O)N2C(C(=O)O)=C(COC(N)=O)…`
ZINC3830484 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CO/N=C(/C(=O)N[C@H]1C(=O)N2C(C(=O)O)=C(COC(N)=O…`
ZINC3830485 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CO/N=C(/C(=O)N[C@@H]1C(=O)N2C(C(=O)O)=C(COC(N)=…`
ZINC3830486 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CO/N=C(/C(=O)N[C@H]1C(=O)N2C(C(=O)O)=C(COC(N)=O…`
ZINC3830487 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CO/N=C(/C(=O)N[C@@H]1C(=O)N2C(C(=O)O)=C(COC(N)=…`
ZINC3871977 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CO/N=C(\C(=O)N[C@H]1C(=O)N2C(C(=O)O)=C(COC(N)=O…`
ZINC3871978 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CO/N=C(\C(=O)N[C@@H]1C(=O)N2C(C(=O)O)=C(COC(N)=…`
ZINC4535978 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CO/N=C(\C(=O)N[C@H]1C(=O)N2C(C(=O)O)=C(COC(N)=O…`
ZINC4574563 ZINC	0.542	424.4 Da LogP -0.54 TPSA 173.8	✓ Ro5	✓ Clean	`CO/N=C(\C(=O)N[C@@H]1C(=O)N2C(C(=O)O)=C(COC(N)=…`
ZINC204907801 ZINC	0.537	425.5 Da LogP 0.61 TPSA 147.2	✓ Ro5	✓ Clean	`CC1=CN2C(=O)[C@@H](NC(=O)/C(=N/OC(C)(C)C(=O)O)c…`
ZINC613829019 ZINC	0.537	425.5 Da LogP 0.61 TPSA 147.2	✓ Ro5	✓ Clean	`CC1=CN2C(=O)[C@@H](NC(=O)C(=NOC(C)(C)C(=O)O)c3c…`
ZINC255975427 ZINC	0.536	383.5 Da LogP 0.66 TPSA 93.4	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(SC3CN(C4=NCC…`
ZINC40721293 ZINC	0.536	383.5 Da LogP 0.66 TPSA 93.4	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1C(=O)N2C(C(=O)O)=C(SC3CN(C4=NCC…`
ZINC584567150 ZINC	0.536	383.5 Da LogP 0.66 TPSA 93.4	✓ Ro5	✓ Clean	`C[C@@H]1C(SC2CN(C3=NCCS3)C2)=C(C(=O)O)N2C(=O)[C…`
ZINC148820510 ZINC	0.518	453.4 Da LogP -1.22 TPSA 201.6	✓ Ro5	✓ Clean	`CC(C)(O/N=C(/C(=O)N[C@@H]1C(=O)N(S(=O)(=O)O)[C@…`
ZINC13520637 ZINC	0.517	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@…`
ZINC4576931 ZINC	0.517	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@@…`

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.