Protein profile

KP13_01582

Peptidoglycan synthase ftsI

Genome: KpKP13

Gene: AHE43893.1 ftsI Structure source: AlphaFold + ColabFold UniProt A0A0H3GVC7

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Amino acids 582

Annotations 12

Features 25

PDB binders 22

Druggability 0.202

Overview

Basic information about this protein and its source genome.

Accession: KP13_01582
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43893.1 ftsI
Status: annotated
Amino acids: 582
Structure source: AlphaFold + ColabFold

3.4.16.4

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:0008658 Binding to penicillin, an antibiotic that contains the condensed beta-lactamthiazolidine ring system. GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. 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:0009002 Catalysis of the reaction: (Ac)2-L-Lys-D-alanyl-D-alanine + H2O = (Ac)2-L-Lys-D-alanine + D-alanine.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 61.217
DEG E-value: 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 91.74

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 0.202

Structure A0A0H3GVC7

Pocket Pocket 1

P2Rank 0.699

Structure A0A0H3GVC7

Pocket Pocket 1

ColabFold model

FPocket 0.097 · Pocket 1

P2Rank 0.728 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 114 / 4744 genomes with a hit

Normalized 0.024

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Enzyme Commission (EC)

3.4.16.4

Gene Ontology (GO)

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:0008658 Binding to penicillin, an antibiotic that contains the condensed beta-lactamthiazolidine ring system.
GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
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: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:0000917 The assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis. The progeny cells that form a division septum are not able to exchange intracellular material.
GO:0043093 A cytokinesis process that involves a set of conserved proteins including FtsZ, and results in the formation of two similarly sized and shaped cells.
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 Features

Domain/signature hits from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
254	548	Pfam	PF00905	Penicillin binding protein transpeptidase domain
254	548	InterPro	IPR001460	Penicillin-binding protein, transpeptidase
7	565	Hamap	MF_02080	Peptidoglycan D,D-transpeptidase FtsI [ftsI].
7	565	InterPro	IPR037532	Peptidoglycan D,D-transpeptidase FtsI
82	155	Gene3D	G3DSA:1.10.150.770	-
10	560	PANTHER	PTHR30627	PEPTIDOGLYCAN D,D-TRANSPEPTIDASE
290	470	FunFam	G3DSA:3.40.710.10:FF:000003	Peptidoglycan D,D-transpeptidase FtsI
290	470	Gene3D	G3DSA:3.40.710.10	-
290	470	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
31	228	Gene3D	G3DSA:3.90.1310.10	-
57	228	SUPERFAMILY	SSF56519	Penicillin binding protein dimerisation domain
57	228	InterPro	IPR036138	Penicillin-binding protein, dimerisation domain superfamily
62	215	Pfam	PF03717	Penicillin-binding Protein dimerisation domain
62	215	InterPro	IPR005311	Penicillin-binding protein, dimerisation domain
40	582	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	18	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
229	557	SUPERFAMILY	SSF56601	beta-lactamase/transpeptidase-like
229	557	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
233	544	Gene3D	G3DSA:3.30.450.330	-
1	39	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	28	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
20	42	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
19	34	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
35	39	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
53	228	FunFam	G3DSA:3.90.1310.10:FF:000003	Peptidoglycan D,D-transpeptidase FtsI

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_A0A0H3GVC7	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01582	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
1				0.202

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	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				10.91	0.585
2				0.99	0.005

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	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				11.64	0.619
2				1.0	0.006

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.

73 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
0W0	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	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	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	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)…`
AXL	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	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	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	6SYN	A0A3N4B5A3	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	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…`
IM2	3PBQ	G3XD46	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	6I1I	P0AD68	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	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…`
ODZ	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	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	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…`
R7G	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	6VJE	G3XD46	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	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…`
TMO	7ONO	P0AD68	75.1 Da LogP 0.19 TPSA 23.1	✓ Ro5	✓ Clean	`C[N+](C)(C)[O-]`
UE1	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	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	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
CHEMBL1359	C3TQQ7	—	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…`

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
ZINC21984184	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	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	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	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	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	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	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	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	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	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)…`
ZINC72481794	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	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	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	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`
ZINC11616761	0.597	461.5 Da LogP 0.09 TPSA 148.1	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](NC(=O)N3CCNC3=…`
ZINC1530561	0.597	461.5 Da LogP 0.09 TPSA 148.1	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@@H](NC(=O)[C@H](NC(=O)N3CCNC3=…`
ZINC2121453	0.597	461.5 Da LogP 0.09 TPSA 148.1	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@@H](NC(=O)[C@H](NC(=O)N3CCNC3=…`
ZINC3830260	0.597	461.5 Da LogP 0.09 TPSA 148.1	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)[C@H](NC(=O)N3CCNC3=O)…`
ZINC3830261	0.597	461.5 Da LogP 0.09 TPSA 148.1	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](NC(=O)N3CCNC3=O…`
ZINC3830262	0.597	461.5 Da LogP 0.09 TPSA 148.1	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](NC(=O)N3CCNC3=O…`
ZINC4097284	0.597	461.5 Da LogP 0.09 TPSA 148.1	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](NC(=O)N3CCNC3=…`
ZINC4534031	0.597	461.5 Da LogP 0.09 TPSA 148.1	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@@H](NC(=O)[C@@H](NC(=O)N3CCNC3=…`
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…`
ZINC1560410105	0.580	433.4 Da LogP -0.70 TPSA 201.6	✓ Ro5	✓ Clean	`CC1=C(NC(=O)C(=NOC(C)(C)C(=O)O)c2csc(N)n2)C(=O)…`
ZINC82265534	0.579	207.3 Da LogP 1.85 TPSA 49.3	✓ Ro5	✓ Clean	`CC(C)(C)NC(=O)Cc1ccc(O)cc1`
ZINC39022681	0.575	263.3 Da LogP 2.71 TPSA 55.4	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)N[C@](C)(C=O)Cc1ccccc1`
ZINC39022682	0.575	263.3 Da LogP 2.71 TPSA 55.4	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)N[C@@](C)(C=O)Cc1ccccc1`
ZINC3792388	0.569	399.5 Da LogP -0.43 TPSA 122.1	✓ Ro5	✓ Clean	`CNCC[C@@H](O)[C@@H]1C[C@H](SC2=C(C(=O)O)N3C(=O)…`
ZINC72481777	0.568	213.3 Da LogP 2.04 TPSA 55.4	✓ Ro5	✓ Clean	`C=C[C@](C)(CC=O)NC(=O)OC(C)(C)C`
ZINC72481778	0.568	213.3 Da LogP 2.04 TPSA 55.4	✓ Ro5	✓ Clean	`C=C[C@@](C)(CC=O)NC(=O)OC(C)(C)C`
ZINC21297226	0.559	273.3 Da LogP 0.39 TPSA 135.1	✓ Ro5	✓ Clean	`CC(C)(O/N=C(\C(=O)O)c1csc(N)n1)C(=O)O`
ZINC21992425	0.559	273.3 Da LogP 0.39 TPSA 135.1	✓ Ro5	✓ Clean	`CC(C)(O/N=C(/C(=O)O)c1csc(N)n1)C(=O)O`
ZINC256007020	0.559	273.3 Da LogP 0.39 TPSA 135.1	✓ Ro5	✓ Clean	`CC(C)(ON=C(C(=O)O)c1csc(N)n1)C(=O)O`
ZINC72481991	0.553	228.3 Da LogP 1.33 TPSA 81.4	✓ Ro5	✓ Clean	`C=C[C@](C)(CC(N)=O)NC(=O)OC(C)(C)C`
ZINC72481992	0.553	228.3 Da LogP 1.33 TPSA 81.4	✓ Ro5	✓ Clean	`C=C[C@@](C)(CC(N)=O)NC(=O)OC(C)(C)C`
ZINC137339669	0.552	353.8 Da LogP 0.60 TPSA 107.0	✓ Ro5	✓ Clean	`CCN1CCN(C(=O)N[C@@H](C(=O)Cl)c2ccc(O)cc2)C(=O)C…`
ZINC15021194	0.550	271.3 Da LogP 0.90 TPSA 114.9	✓ Ro5	Alert	`CC(=O)/C(=N\OC(C)(C)C(=O)O)c1csc(N)n1`
ZINC15848211	0.542	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	0.542	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	0.542	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	0.542	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…`
ZINC256010241	0.542	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	0.542	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(…`
ZINC3830266	0.542	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(…`

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.