KpKP13 Protein target profile

Peptidoglycan synthase ftsI

Accession: KP13_01911

Gene: AHE46352.1 3D evidence: Experimental + ColabFold model UniProt A0A0H3GN85

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Length 588

Pocket druggability (P2Rank · Experimental) 0.52

Direct ligand evidence 0 76 total records

Functional annotation 1 EC 11 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.52, FPocket 0.76). Use the 3D pocket comparison to verify whether they identify the same site. Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. 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. Review the complete evidence below

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

Structure confidence

ColabFold pLDDT: 90.76 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

PDB experimental structure

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.52

Structure 8GPW

Pocket Pocket 1

Druggability (FPocket) 0.756

Structure 8GPW

Pocket Pocket 1

ColabFold model

P2Rank 0.732 · Pocket 1

FPocket 0.53 · Pocket 9

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 140 / 4744 genomes with a hit

Prevalence 3.0%

Sequence

Primary amino-acid sequence viewer.

MKAAPKTPKAKRQEEQANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVRQGDMRSLRVQEVSTARGMITDRSGRPLAVSVPVKAIWADPKELHDAGGVTLDTRWKALADALNMPLDQLATRINTNPRMRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNFAGTAKDTMRNRAITDVFEPGSTVKPMVVMTALQRGIVNENTVLNTVPYRINGHEIKDVARYSELTLTGVLQKSSNVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQRWSDIERATFSFGYGLMVTPLQLARVYATIGSYGIYRPLSITKVDPPVPGERVFPESLVRTVVHMMESVALPGGGGVKAAIKGYRIAIKTGTAKKVGPDGRYINKYIAYTAGVAPASHPRFALVVVINDPQAGKYYGGAVSAPVFGAIMGGVLRTMNIEPDALATGEKSEFVINQGEGTGGRS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Subcellular localization

Localization: CytoplasmicMembrane

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 domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
59	234	FunFam	G3DSA:3.90.1310.10:FF:000003	Peptidoglycan D,D-transpeptidase FtsI
21	43	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
296	476	Gene3D	G3DSA:3.40.710.10	-
296	476	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
88	160	FunFam	G3DSA:1.10.150.770:FF:000001	Peptidoglycan D,D-transpeptidase FtsI
1	19	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
239	550	Gene3D	G3DSA:3.30.450.330	-
45	588	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
235	563	SUPERFAMILY	SSF56601	beta-lactamase/transpeptidase-like
235	563	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
63	233	SUPERFAMILY	SSF56519	Penicillin binding protein dimerisation domain
63	233	InterPro	IPR036138	Penicillin-binding protein, dimerisation domain superfamily
296	476	FunFam	G3DSA:3.40.710.10:FF:000003	Peptidoglycan D,D-transpeptidase FtsI
88	160	Gene3D	G3DSA:1.10.150.770	-
13	575	Hamap	MF_02080	Peptidoglycan D,D-transpeptidase FtsI [ftsI].
13	575	InterPro	IPR037532	Peptidoglycan D,D-transpeptidase FtsI
20	44	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
14	567	PANTHER	PTHR30627	PEPTIDOGLYCAN D,D-TRANSPEPTIDASE
260	554	Pfam	PF00905	Penicillin binding protein transpeptidase domain
260	554	InterPro	IPR001460	Penicillin-binding protein, transpeptidase
70	220	Pfam	PF03717	Penicillin-binding Protein dimerisation domain
70	220	InterPro	IPR005311	Penicillin-binding protein, dimerisation domain
38	234	Gene3D	G3DSA:3.90.1310.10	-

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

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.52

Likely same site as FPocket 1 2.4 Å 14 shared residues 78% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.044

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Surrounding area

Pocket 3 P2Rank #3

0.006

Likely same site as FPocket 4 6.2 Å 8 shared residues 89% of smaller site

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.756 Unusual size

Likely same site as P2Rank 1 2.4 Å 14 shared residues 78% of smaller site

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Surrounding area

Pocket 2 FPocket #4

0.249

Likely same site as P2Rank 3 6.2 Å 8 shared residues 89% of smaller site

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Surrounding area

Pocket 3 FPocket #16

0.204

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.732

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Surrounding area

Pocket 2 P2Rank #2

0.07

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Surrounding area

Pocket 3 P2Rank #3

0.016

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Surrounding area

Pocket 4 P2Rank #4

0.005

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Surrounding area

All structural evidence 1 experimental · 1 predicted

Structural evidence

1 + 1

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
PDB 8GPW	X-ray	2.06 Å	A,B	69.2% 164-570	PDBe RCSB PDBj File	Viewing
ColabFold KP13_01911	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.

76 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 26 records from similar proteins

Structural ligands 25 0 loaded crystals

Measured bioactivity 1 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

3LB PDB via homolog Detail RCSB PDB

3LC PDB via homolog Detail RCSB PDB

3LE PDB via homolog Detail RCSB PDB

59F 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…`
3LB RCSB PDB	4WEJ	A0A0M3KKZ3	802.8 Da LogP -2.82 TPSA 342.9	3 viol.	✓ Clean	`CC(C)(C(=O)O)ON=C(c1csc(n1)N)C(=O)N[C@H](C=O)[C…`
3LC RCSB PDB	4WEK	A0A0M3KKZ4	788.8 Da LogP -2.41 TPSA 342.9	3 viol.	✓ Clean	`CC(C)(C(=O)O)O/N=C(/c1csc(n1)N)\C(=O)N[C@H](C=O…`
3LE RCSB PDB	4WEL	A0A0M3KKZ3	776.8 Da LogP -2.57 TPSA 342.9	3 viol.	✓ Clean	`C[C@@H]([C@@H](C=O)NC(=O)/C(=N\OC(C)(C)C(=O)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)…`
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…`
IM2 RCSB PDB	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 RCSB PDB	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 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…`
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…`
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	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 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…`
TMO RCSB PDB	7ONO	P0AD68	75.1 Da LogP 0.19 TPSA 23.1	✓ Ro5	✓ Clean	`C[N+](C)(C)[O-]`
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
CHEMBL1359 ChEMBL	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
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…`
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…`
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)…`
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`
ZINC82265534 ZINC	0.579	207.3 Da LogP 1.85 TPSA 49.3	✓ Ro5	✓ Clean	`CC(C)(C)NC(=O)Cc1ccc(O)cc1`
ZINC4262525 ZINC	0.578	319.3 Da LogP 0.21 TPSA 107.0	✓ Ro5	✓ Clean	`CCN1CCN(C(=O)N[C@@H](C(=O)O)c2ccccc2)C(=O)C1=O`
ZINC4977719 ZINC	0.578	319.3 Da LogP 0.21 TPSA 107.0	✓ Ro5	✓ Clean	`CCN1CCN(C(=O)N[C@H](C(=O)O)c2ccccc2)C(=O)C1=O`
ZINC39022681 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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`
ZINC13831148 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC1535361 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@@H]1C(S[C@H]2CN[C@@H](CNS(N)(=O)=O)C2)=C(C(…`
ZINC21985895 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1C(=O)N2C(C(=O)O)=C(S[C@H]3CN[C@…`
ZINC252446781 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC252446782 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@@H]1C(S[C@@H]2CN[C@H](CNS(N)(=O)=O)C2)=C(C(…`
ZINC252446783 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC36584727 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@H]1C(S[C@H]2CN[C@@H](CNS(N)(=O)=O)C2)=C(C(=…`
ZINC36584729 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1C(=O)N2C(C(=O)O)=C(S[C@H]3CN[C…`
ZINC36584731 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@@H]1C(S[C@H]2CN[C@@H](CNS(N)(=O)=O)C2)=C(C(…`
ZINC3922770 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1C(=O)N2C(C(=O)O)=C(S[C@@H]3CN[C…`
ZINC55161939 ZINC	0.562	420.5 Da LogP -1.60 TPSA 162.1	✓ Ro5	✓ Clean	`C[C@H]1C(S[C@@H]2CN[C@H](CNS(N)(=O)=O)C2)=C(C(=…`
ZINC21297226 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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`
ZINC15021194 ZINC	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`
ZINC16958002 ZINC	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(…`
ZINC256010241 ZINC	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…`
ZINC3830266 ZINC	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.

Cross-references

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