KpATCC43816 Protein target profile

penicillin-binding protein 1B

Accession: VK055_2402

Gene: AIK80999.1 mrcB 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GIH5

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Length 851

Pocket druggability (P2Rank · AlphaFold DB model) 0.723

Direct ligand evidence 0 62 total records

Functional annotation 0 EC 12 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 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: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 47.908 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 86.47 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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) 0.723

Structure A0A0H3GIH5

Pocket Pocket 1

Druggability (FPocket) 0.761

Structure A0A0H3GIH5

Pocket Pocket 15

ColabFold model

P2Rank 0.76 · Pocket 1

FPocket 0.269 · Pocket 18

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 109 / 4744 genomes with a hit

Prevalence 2.3%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MAGDDREPIGRKGRPSRPTKQKVTRRRVREEDYDDEYDDDDYEDEKPVPRKAKGKGGKPRRKRSWLWLLVKLGIVFAVLIAAYGVYLDQKIRSRIDGKVWELPAAVYGRMVNLEPDMQISKNEMVRLLNATQYRQVSAMTRPGEYTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHLETIENMDNNRQFGFFRLDPRLITMLQSPNGEQRLFVKRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIVDARYSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASVYNPWRNPKLALERRNLVLRLLQQQQVIDQELYDMLSARPLGVQPRGGVISPQPAFMQMVRQELQAKLGDKVKDLSGVKIFTTFDSVAQDAAEKAASEGIPVLKKQRKLADLETAMVVVDRFTGEVRAMVGGAEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPNQYRLNTWIADAPVTIRLSNGQTWSPQNDDRRFSGQVMLVDALTRSMNVPTVNLGMALGLPAVVDTWTKLGAPKNQLNAVPSMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGTVLYQSYPQAERAVPAQAAYMTLWTMQQVVQRGTGRQLGAKYPGLHLAGKTGTTNNNVDTWFAGIDGSQVTITWVGRDNNQPTKLYGASGAMSIYQRYLANQTPTPLVLTVPEDVVDMGVDSNGNFVCSGGMRSLPVWTTQPDALCRQGEMMQQQQLQQQEAKNPFNQSGQQPPPQQQQQQQQPPKQQEKSDGVAGWIKDMFGSN

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

12 GO

Subcellular localization

Localization: CytoplasmicMembrane

Gene Ontology (GO)

GO:0008658 Binding to penicillin, an antibiotic that contains the condensed beta-lactamthiazolidine ring system.
GO:0008233 Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
GO:0009274 A protective structure outside the cytoplasmic membrane composed of peptidoglycan (also known as murein), a molecule made up of a glycan (sugar) backbone of repetitively alternating N-acetylglucosamine and N-acetylmuramic acid with short, attached, cross-linked peptide chains containing unusual amino acids. An example of this component is found in Escherichia coli.
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: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.
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: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: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.

32 records

Show feature table

Start	End	DB	Term	Name
196	403	SUPERFAMILY	SSF53955	Lysozyme-like
196	403	InterPro	IPR023346	Lysozyme-like domain superfamily
113	197	Pfam	PF14814	Bifunctional transglycosylase second domain
113	197	InterPro	IPR028166	Bifunctional transglycosylase second domain
87	851	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
111	200	Gene3D	G3DSA:3.30.2060.10	-
1	64	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
398	767	FunFam	G3DSA:3.40.710.10:FF:000006	Penicillin-binding protein 1B
209	380	Pfam	PF00912	Transglycosylase
209	380	InterPro	IPR001264	Glycosyl transferase, family 51
795	835	MobiDBLite	mobidb-lite	consensus disorder prediction
58	96	Gene3D	G3DSA:1.20.5.100	-
201	404	FunFam	G3DSA:1.10.3810.10:FF:000002	Penicillin-binding protein 1B
103	767	Gene3D	G3DSA:3.40.710.10	-
103	767	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
65	87	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
473	713	Pfam	PF00905	Penicillin binding protein transpeptidase domain
473	713	InterPro	IPR001460	Penicillin-binding protein, transpeptidase
201	404	Gene3D	G3DSA:1.10.3810.10	-
201	404	InterPro	IPR036950	Penicillin binding protein transglycosylase domain
68	792	NCBIfam	TIGR02071	penicillin-binding protein 1B
68	792	InterPro	IPR011813	Penicillin-binding protein 1B
46	836	PANTHER	PTHR32282	BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED
1	79	Pfam	PF14812	Transmembrane domain of transglycosylase PBP1 at N-terminal
1	79	InterPro	IPR032730	Transglycosylase PBP1b, N-terminal transmembrane domain
36	849	PIRSF	PIRSF002799	PBP1b
36	849	InterPro	IPR011813	Penicillin-binding protein 1B
65	86	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
795	851	MobiDBLite	mobidb-lite	consensus disorder prediction
362	788	SUPERFAMILY	SSF56601	beta-lactamase/transpeptidase-like
362	788	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
1	56	MobiDBLite	mobidb-lite	consensus disorder prediction

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

0.723

Likely same site as FPocket 15 2.5 Å 19 shared residues 83% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.46

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Surrounding area

Pocket 3 P2Rank #3

0.306

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Surrounding area

Pocket 4 P2Rank #4

0.107

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Surrounding area

Pocket 5 P2Rank #5

0.06

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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 #15

0.761 Unusual size

Likely same site as P2Rank 1 2.5 Å 19 shared residues 83% of smaller site

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Surrounding area

Pocket 2 FPocket #36

0.214

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Surrounding area

Residue sets

UniProt: Active site:233-233 Proton donor; for transglycosylase activity

UniProt: Active site:510-510 Acyl-ester intermediate; for transpeptidase activity

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.76

Likely same site as FPocket 18 1.8 Å 26 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.439

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Surrounding area

Pocket 3 P2Rank #3

0.364

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Surrounding area

Pocket 4 P2Rank #4

0.084

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Surrounding area

Pocket 5 P2Rank #5

0.052

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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_A0A0H3GIH5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2402	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.

62 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 12 records from similar proteins

Structural ligands 12 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5VW PDB via homolog 352.4 Da · LogP -2.29 · TPSA 146.3 Open detail RCSB PDB

63U PDB via homolog Detail RCSB PDB

63V PDB via homolog Detail RCSB PDB

AIX PDB via homolog Detail RCSB PDB

AZR 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
5VW RCSB PDB	5FGZ	P02919	352.4 Da LogP -2.29 TPSA 146.3	✓ Ro5	✓ Clean	`C1C[C@H](N(C[C@@H]1NOS(=O)(=O)O)C=O)C(=O)NO[C@H…`
63U RCSB PDB	5HLA	P02919	349.4 Da LogP 0.39 TPSA 121.5	✓ Ro5	✓ Clean	`CC1=C(N[C@@H](SC1)[C@@H](C=O)NC(=O)[C@@H](c2ccc…`
63V RCSB PDB	5HLD	P02919	338.4 Da LogP 1.13 TPSA 95.8	✓ Ro5	✓ Clean	`C=C1CS[C@H](N=C1C(=O)O)[C@@H](C=O)NC(=O)Cc2cccs2`
AIX RCSB PDB	5HL9	P02919	351.4 Da LogP 0.26 TPSA 121.5	✓ Ro5	✓ Clean	`CC1([C@@H](N[C@H](S1)[C@@H](C=O)NC(=O)[C@@H](c2…`
AZR RCSB PDB	5HLB	P02919	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…`
LDA RCSB PDB	3DWK	Q8KHY3	229.4 Da LogP 4.48 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)[O-]`
M0E RCSB PDB	3FWL	P02919	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…`
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`

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).

No ChEMBL hits found through similar proteins.

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 ZINC	1.000	201.4 Da LogP 3.70 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)[O-]`
ZINC2008702 ZINC	1.000	243.4 Da LogP 4.87 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC[N+](C)(C)[O-]`
ZINC2039372 ZINC	1.000	229.4 Da LogP 4.48 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)[O-]`
ZINC2516963 ZINC	1.000	215.4 Da LogP 4.09 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCC[N+](C)(C)[O-]`
ZINC34064299 ZINC	0.725	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)…`
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`
ZINC1673414 ZINC	0.600	228.4 Da LogP 4.61 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)C`
ZINC1700269 ZINC	0.600	200.4 Da LogP 3.83 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)C`
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)…`
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`
ZINC1560410105 ZINC	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)…`
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`
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`
ZINC100991279 ZINC	0.548	314.5 Da LogP 4.38 TPSA 52.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)NCCCC[N+](C)(C)[O-]`
ZINC1670600 ZINC	0.545	201.4 Da LogP 3.08 TPSA 26.0	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)N`
ZINC59314569 ZINC	0.545	229.4 Da LogP 3.86 TPSA 26.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)N`
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)=…`
ZINC15848211 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(…`
ZINC252430978 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)n…`
ZINC256010240 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)…`
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…`
ZINC3830263 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(…`
ZINC3830264 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(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.

Cross-references

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

Sequence

UniProt A0A0H3GIH5