Protein profile

VK055_4651

penicillin-binding protein 1C

Genome: KpATCC43816

Gene: pbpC AIK83185.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3H1G6

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Amino acids 771

Annotations 7

Features 26

PDB binders 8

Druggability 0.635

Overview

Basic information about this protein and its source genome.

Accession: VK055_4651
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: pbpC AIK83185.1
Status: annotated
Amino acids: 771
Structure source: AlphaFold + ColabFold

2.4.99.28

GO:0008658 Binding to penicillin, an antibiotic that contains the condensed beta-lactamthiazolidine ring system. 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: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: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:0004180 Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain. GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 38.514
Localization: CytoplasmicMembrane
ColabFold pLDDT: 90.04

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.635

Structure A0A0H3H1G6

Pocket Pocket 9

P2Rank 0.405

Structure A0A0H3H1G6

Pocket Pocket 1

ColabFold model

FPocket 0.562 · Pocket 21

P2Rank 0.303 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 100 / 4744 genomes with a hit

Normalized 0.021

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

2.4.99.28

Gene Ontology (GO)

GO:0008658 Binding to penicillin, an antibiotic that contains the condensed beta-lactamthiazolidine ring system.
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: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: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:0004180 Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain.
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
248	592	FunFam	G3DSA:3.40.710.10:FF:000021	Penicillin-binding protein 1C
10	20	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
21	24	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
685	765	Pfam	PF06832	Penicillin-Binding Protein C-terminus Family
685	765	InterPro	IPR009647	Penicillin-binding, C-terminal
25	771	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
52	246	Gene3D	G3DSA:1.10.3810.10	-
52	246	InterPro	IPR036950	Penicillin binding protein transglycosylase domain
249	574	Gene3D	G3DSA:3.40.710.10	-
249	574	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
9	566	PANTHER	PTHR32282	BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED
1	9	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
38	255	SUPERFAMILY	SSF53955	Lysozyme-like
38	255	InterPro	IPR023346	Lysozyme-like domain superfamily
299	515	Pfam	PF00905	Penicillin binding protein transpeptidase domain
299	515	InterPro	IPR001460	Penicillin-binding protein, transpeptidase
1	24	Phobius	SIGNAL_PEPTIDE	Signal peptide region
53	247	FunFam	G3DSA:1.10.3810.10:FF:000006	Penicillin-binding protein 1C
35	769	NCBIfam	TIGR02073	penicillin-binding protein 1C
35	769	InterPro	IPR011815	Penicillin-binding protein 1C
205	639	SUPERFAMILY	SSF56601	beta-lactamase/transpeptidase-like
205	639	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
7	29	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	25	SignalP_EUK	SignalP-noTM	SignalP-noTM
57	223	Pfam	PF00912	Transglycosylase
57	223	InterPro	IPR001264	Glycosyl transferase, family 51

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3H1G6	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_4651	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
46				0.143
1				0.005
40				0.001
47				0.0

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	8.83	0.405
2	3.56	0.106
3	2.99	0.078
4	2.19	0.043
5	1.79	0.028

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
50				0.046
1				0.005
30				0.001
54				0.001

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	6.99	0.303
2	3.61	0.108
3	3.0	0.079
4	2.48	0.056
5	2.24	0.045

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.

65 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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…`
35P	5CXW	P71707	352.4 Da LogP 0.64 TPSA 104.7	✓ Ro5	✓ Clean	`CC1([C@@H](N[C@H](S1)[C@@H](C=O)NC(=O)COc2ccccc…`
BMG	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	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	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…`
LDA	3DWK	Q8KHY3	229.4 Da LogP 4.48 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)[O-]`
TEB	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	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`

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	Q07806	7.52	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	Q07806	7.34	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	Q07806	7.34	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	Q07806	7.34	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	Q07806	7.34	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	Q07806	7.19	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	Q07806	6.96	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
ZINC1849937	1.000	201.4 Da LogP 3.70 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)[O-]`
ZINC2008702	1.000	243.4 Da LogP 4.87 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC[N+](C)(C)[O-]`
ZINC2039372	1.000	229.4 Da LogP 4.48 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)[O-]`
ZINC2516963	1.000	215.4 Da LogP 4.09 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCC[N+](C)(C)[O-]`
ZINC65748378	0.741	368.4 Da LogP 0.53 TPSA 125.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]([C@H](NC(=O)COc2ccccc2)C(=O)O)N[C…`
ZINC12359024	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	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	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	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	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	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	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	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	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`
ZINC1673414	0.600	228.4 Da LogP 4.61 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)C`
ZINC1700269	0.600	200.4 Da LogP 3.83 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)C`
ZINC255982699	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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…`
ZINC100991279	0.548	314.5 Da LogP 4.38 TPSA 52.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)NCCCC[N+](C)(C)[O-]`
ZINC1670600	0.545	201.4 Da LogP 3.08 TPSA 26.0	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)N`
ZINC59314569	0.545	229.4 Da LogP 3.86 TPSA 26.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)N`
ZINC254005599	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	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	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…`
ZINC3830484	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	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	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	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	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	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	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	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)=…`

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.