KpATCC43816 Protein target profile

gamma-glutamyltransferase

Accession: VK055_3663

Gene: AIK82218.1 ggt 3D evidence: AlphaFold DB model + ColabFold model Metabolism 13 reactions UniProt A0A0H3GWX6

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Length 580

Pocket druggability (P2Rank · AlphaFold DB model) 0.711

Metabolic reactions 13

Chokepoint No

Direct ligand evidence 0 58 total records

Functional annotation 2 EC 4 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.44. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.71. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

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: Hit
Human identity (%): 40.876 Lower values reduce human off-target concern.
Human E-value: 2.38e-24
Gut microbiome similarity: 2.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 88.793 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 91.1 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) 0.711

Structure A0A0H3GWX6

Pocket Pocket 1

Druggability (FPocket) 0.442

Structure A0A0H3GWX6

Pocket Pocket 6

ColabFold model

P2Rank 0.66 · Pocket 1

FPocket 0.209 · Pocket 10

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 104 / 4744 genomes with a hit

Prevalence 2.2%

Metabolic context

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

Explore metabolic network

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MIKTTIWRQVVIAALLAGGSFTVAANPPPPPVSYGVEEDVFHPVRARQGMVASVDALATRVGVDILRQGGNAVDAAVAVGYALAVTHPQAGNIGGGGFMMLRTKDGKTTAIDFREMAPEQATRDMFLDDQGNPDSKKSLTSHLASGTPGSVAGFSLALEKYGTMPLNKVIRPAIKLAEEGFIVNDALADDLKTYGSEVIPQHENSKAIFWKNGEPLKKGDRLVQKNLGKSLELIAEHGPDAFYKGAIADQIADEMKKHGGLITKADLAGYKAVERTPVSGEYRGYEVYSMPPPSSGGIHIVQILNILENFDMQKYGFGSADAMQVMAEAEKHAYADRSEYLGDPDFVNVPWQALTSKAYAKAIAAEIDVNKAKPSSQIRPGKLAPYESNQTTHFSVVDKDGNAVAVTYTLNTTFGTGIVAGDSGILLNNQMDDFSAKPGVPNVYGLVGGEANAVEPKKRPLSSMSPTIVVKDGKTWLVTGSPGGSRIITTVLQMVVNTIDFGMNVAEATNAPRFHHQWLPDELRVEKGFSPDTLKLLEAKGQKVALKEAMGSTQSIMVGPDGMLYGASDPRSPDDLTAGY

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 4 GO

Subcellular localization

Localization: Periplasmic

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0006751 The chemical reactions and pathways resulting in the breakdown of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins.
GO:0036374 Catalysis of the reaction: glutathione + H2O = L-cysteinylglycine + L-glutamate.
GO:0103068 OBSOLETE. Catalysis of the reaction: leukotriene C4 + a standard alpha amino acid = leukotriene D4 + an (gamma-L-glutamyl)-L-amino acid.
GO:0006750 The chemical reactions and pathways resulting in the formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

30 records

Show feature table

Start	End	DB	Term	Name
64	572	Pfam	PF01019	Gamma-glutamyltranspeptidase
277	390	Gene3D	G3DSA:1.10.246.130	-
277	390	InterPro	IPR043138	Gamma-glutamyltranspeptidase, large subunit, C-terminal domain
22	25	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	25	Phobius	SIGNAL_PEPTIDE	Signal peptide region
42	572	PANTHER	PTHR43199	GLUTATHIONE HYDROLASE
1	9	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
391	580	Gene3D	G3DSA:3.60.20.40	-
391	580	InterPro	IPR043137	Gamma-glutamyltranspeptidase, small subunit
26	580	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
277	390	FunFam	G3DSA:1.10.246.130:FF:000004	Gamma-glutamyltranspeptidase (Ggt)
1	25	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
49	571	NCBIfam	TIGR00066	gamma-glutamyltransferase
49	571	InterPro	IPR000101	Gamma-glutamyltranspeptidase
41	573	SUPERFAMILY	SSF56235	N-terminal nucleophile aminohydrolases (Ntn hydrolases)
41	573	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
1	25	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
391	415	ProSitePatterns	PS00462	Gamma-glutamyltranspeptidase signature.
391	415	InterPro	IPR000101	Gamma-glutamyltranspeptidase
10	21	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
291	310	PRINTS	PR01210	Gamma-glutamyltranspeptidase signature
480	497	PRINTS	PR01210	Gamma-glutamyltranspeptidase signature
162	181	PRINTS	PR01210	Gamma-glutamyltranspeptidase signature
391	409	PRINTS	PR01210	Gamma-glutamyltranspeptidase signature
71	96	PRINTS	PR01210	Gamma-glutamyltranspeptidase signature
261	277	PRINTS	PR01210	Gamma-glutamyltranspeptidase signature
415	433	PRINTS	PR01210	Gamma-glutamyltranspeptidase signature
456	471	PRINTS	PR01210	Gamma-glutamyltranspeptidase signature
144	162	PRINTS	PR01210	Gamma-glutamyltranspeptidase signature
391	580	FunFam	G3DSA:3.60.20.40:FF:000003	Gamma-glutamyltranspeptidase

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

0.711

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Surrounding area

Pocket 2 P2Rank #2

0.185

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Surrounding area

Pocket 3 P2Rank #3

0.184

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Surrounding area

Pocket 4 P2Rank #4

0.069

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Surrounding area

Pocket 5 P2Rank #5

0.043

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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 #6

0.442

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Surrounding area

Residue sets

UniProt: Active site:392-392 Nucleophile

UniProt: Binding site:115-115

UniProt: Binding site:410-412

UniProt: Binding site:434-434

UniProt: Binding site:463-464

UniProt: Binding site:485-485

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.66

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Surrounding area

Pocket 2 P2Rank #2

0.147

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Surrounding area

Pocket 3 P2Rank #3

0.101

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Surrounding area

Pocket 4 P2Rank #4

0.073

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Surrounding area

Pocket 5 P2Rank #5

0.064

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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 #10

0.209

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Surrounding area

Pocket 2 FPocket #14

0.206

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Surrounding area

Residue sets

UniProt: Active site:392-392 Nucleophile

UniProt: Binding site:115-115

UniProt: Binding site:410-412

UniProt: Binding site:434-434

UniProt: Binding site:463-464

UniProt: Binding site:485-485

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_A0A0H3GWX6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3663	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.

58 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

4UD PDB via homolog 144.1 Da · LogP -0.83 · TPSA 84.9 Open detail RCSB PDB

6FY PDB via homolog Detail RCSB PDB

AVN PDB via homolog Detail RCSB PDB

AZS PDB via homolog Detail RCSB PDB

DON 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
4UD RCSB PDB	5BPK	O25743	144.1 Da LogP -0.83 TPSA 84.9	✓ Ro5	✓ Clean	`C1C=NO[C@@H]1[C@@H](C(=O)O)N`
6FY RCSB PDB	5B5T	P18956	310.2 Da LogP -0.74 TPSA 156.0	✓ Ro5	✓ Clean	`CC[C@H](C(=O)NCC(=O)O)O[P@H](=O)CC[C@@H](C(=O)O…`
AVN RCSB PDB	3FNM	O25743	178.6 Da LogP -0.26 TPSA 84.9	✓ Ro5	✓ Clean	`C1[C@H](ON=C1Cl)[C@@H](C(=O)O)N`
AZS RCSB PDB	2Z8I	P18956	173.1 Da LogP -1.76 TPSA 126.0	✓ Ro5	Alert	`C([C@@H](C(=O)O)N)OC(=O)C=[N+]=[N-]`
DON RCSB PDB	5Y9B	Q65KZ6	173.2 Da LogP -0.22 TPSA 116.6	✓ Ro5	Alert	`C(CC(=O)CN=N)[C@@H](C(=O)O)N`
GBL RCSB PDB	7D9X	A0A6G6IRK3	86.1 Da LogP 0.32 TPSA 26.3	✓ Ro5	✓ Clean	`C1CC(=O)OC1`
GGL RCSB PDB	2DBW	P18956	147.1 Da LogP -0.74 TPSA 100.6	✓ Ro5	✓ Clean	`C(CC(=O)O)[C@@H](C(=O)O)N`
GTB RCSB PDB	2QMC	O25743	442.5 Da LogP -0.29 TPSA 202.0	✓ Ro5	✓ Clean	`c1cc(ccc1CSC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[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).

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
ZINC2031112 ZINC	0.824	200.2 Da LogP 1.43 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCC(=O)OCCCCO1`
ZINC113251999 ZINC	0.778	228.3 Da LogP 2.21 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCC(=O)OCCCCCCO1`
ZINC34542648 ZINC	0.778	228.3 Da LogP 2.21 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCCOC(=O)CCCCCO1`
ZINC4023310 ZINC	0.778	212.3 Da LogP 3.83 TPSA 26.3	✓ Ro5	✓ Clean	`O=C1CCCCCCCCCCCCO1`
ZINC4023520 ZINC	0.778	240.4 Da LogP 4.61 TPSA 26.3	✓ Ro5	✓ Clean	`O=C1CCCCCCCCCCCCCCO1`
ZINC4026026 ZINC	0.778	256.3 Da LogP 2.99 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCCCCCC(=O)OCCCCO1`
ZINC4026253 ZINC	0.778	284.4 Da LogP 3.77 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCCCCCC(=O)OCCCCCCO1`
ZINC4026492 ZINC	0.778	270.4 Da LogP 3.38 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCCCCCC(=O)OCCCCCO1`
ZINC4676827 ZINC	0.778	270.4 Da LogP 3.38 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCCCCC(=O)OCCCCCCO1`
ZINC33802904 ZINC	0.765	344.4 Da LogP 1.29 TPSA 105.2	✓ Ro5	✓ Clean	`O=C1CCCCC(=O)OCCOC(=O)CCCCC(=O)OCCO1`
ZINC35906424 ZINC	0.765	344.4 Da LogP 1.29 TPSA 105.2	✓ Ro5	✓ Clean	`O=C1CCC(=O)OCCCCOC(=O)CCC(=O)OCCCCO1`
ZINC4026344 ZINC	0.750	254.4 Da LogP 3.79 TPSA 43.4	✓ Ro5	✓ Clean	`O=C1CCCCCCCCCCC(=O)OCCC1`
ZINC196715962 ZINC	0.722	456.6 Da LogP 4.41 TPSA 105.2	✓ Ro5	✓ Clean	`O=C1CCCCCCCCC(=O)OCCOC(=O)CCCCCCCCC(=O)OCCO1`
ZINC4015272 ZINC	0.722	228.3 Da LogP 2.21 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCCCCCC(=O)OCCO1`
ZINC4024376 ZINC	0.722	270.4 Da LogP 3.38 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCCCCCCCCC(=O)OCCO1`
ZINC4026271 ZINC	0.722	214.3 Da LogP 1.82 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCCCCC(=O)OCCO1`
ZINC4794429 ZINC	0.722	256.3 Da LogP 2.99 TPSA 52.6	✓ Ro5	✓ Clean	`O=C1CCCCCCCCCCC(=O)OCCO1`
ZINC3870210 ZINC	0.698	473.4 Da LogP -0.53 TPSA 245.1	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CSc1ccc([N+](=O)[O-])cc1…`
ZINC2106542 ZINC	0.667	245.3 Da LogP 1.99 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCCCCCC(=O)O)C(=O)O`
ZINC2106543 ZINC	0.667	245.3 Da LogP 1.99 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCCCCCC(=O)O)C(=O)O`
ZINC2108713 ZINC	0.667	217.3 Da LogP 1.21 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCCCC(=O)O)C(=O)O`
ZINC2108714 ZINC	0.667	217.3 Da LogP 1.21 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCCCC(=O)O)C(=O)O`
ZINC3881672 ZINC	0.667	256.4 Da LogP 3.85 TPSA 35.5	✓ Ro5	✓ Clean	`O=C1CCCCCCCCCCOCCCCO1`
ZINC4026039 ZINC	0.667	256.4 Da LogP 3.85 TPSA 35.5	✓ Ro5	✓ Clean	`O=C1CCCCCCCCCOCCCCCO1`
ZINC5189357 ZINC	0.667	256.4 Da LogP 3.85 TPSA 35.5	✓ Ro5	✓ Clean	`O=C1CCCCCCCCOCCCCCCO1`
ZINC139862480 ZINC	0.650	304.3 Da LogP 0.70 TPSA 80.3	✓ Ro5	✓ Clean	`O=C1CCCCC(=O)OCCOCCOCCOCCO1`
ZINC5188445 ZINC	0.650	216.2 Da LogP 0.66 TPSA 61.8	✓ Ro5	✓ Clean	`O=C1CCCCC(=O)OCCOCCO1`
ZINC2242694 ZINC	0.643	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC2547582 ZINC	0.643	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC4096970 ZINC	0.643	405.4 Da LogP -2.04 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CCC(=O)N[C@@H](CCC(=O)O)…`
ZINC4545890 ZINC	0.643	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC4545891 ZINC	0.643	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC3055005 ZINC	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007 ZINC	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010 ZINC	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC4024200 ZINC	0.619	300.4 Da LogP 3.00 TPSA 61.8	✓ Ro5	✓ Clean	`O=C1CCCCCCCCCCC(=O)OCCOCCO1`
ZINC4863091 ZINC	0.619	316.4 Da LogP 2.24 TPSA 71.1	✓ Ro5	✓ Clean	`O=C1CCCCCCCCC(=O)OCCOCCOCCO1`
ZINC18024709 ZINC	0.600	269.4 Da LogP 4.05 TPSA 58.9	✓ Ro5	✓ Clean	`O=C1CCCCCCCCCC/C(=N\O)CCCO1`
ZINC72334032 ZINC	0.600	241.3 Da LogP 3.27 TPSA 58.9	✓ Ro5	✓ Clean	`O=C1CCCCCCCC/C(=N\O)CCCO1`
ZINC13537379 ZINC	0.593	256.3 Da LogP 1.24 TPSA 106.5	✓ Ro5	✓ Clean	`N[C@@H](CSCc1ccc([N+](=O)[O-])cc1)C(=O)O`
ZINC1530265 ZINC	0.593	219.2 Da LogP -0.80 TPSA 126.9	✓ Ro5	✓ Clean	`N[C@H](CCOC(=O)CCC(=O)O)C(=O)O`
ZINC1532858 ZINC	0.593	219.2 Da LogP -0.80 TPSA 126.9	✓ Ro5	✓ Clean	`N[C@@H](CCOC(=O)CCC(=O)O)C(=O)O`
ZINC1576202 ZINC	0.593	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)NCC(=O)O)C(=O)O`
ZINC1680890 ZINC	0.593	256.3 Da LogP 1.24 TPSA 106.5	✓ Ro5	✓ Clean	`N[C@H](CSCc1ccc([N+](=O)[O-])cc1)C(=O)O`
ZINC3995565 ZINC	0.593	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)NCC(=O)O)C(=O)O`
ZINC1555366 ZINC	0.591	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1555367 ZINC	0.591	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1555369 ZINC	0.591	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720127 ZINC	0.591	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1720128 ZINC	0.591	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`

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 A0A0H3GWX6

Pathways

BioCyc RXN-18092[CCO-CYTOSOL]-GLYCYLGLYCINE/GLUTATHIONE//CPD-19395/CYS-GLY.58. BioCyc RXN-18092[CCO-PERI-BAC]-GLYCYLGLYCINE/GLUTATHIONE//CPD-19395/CYS-GLY.59. BioCyc RXN-23012-CPD-25483/CYS//L-GAMMA-GLUTAMYLCYSTEINE/CPD-25489.50. BioCyc RXN-23012-CPD-25483/L-ALPHA-ALANINE//CPD-22081/CPD-25489.47. BioCyc RXN-23014-CPD-25481/CYS//CPD-25491/L-GAMMA-GLUTAMYLCYSTEINE.50. BioCyc RXN-23014-CPD-25481/L-ALPHA-ALANINE//CPD-25491/CPD-22081.47. BioCyc RXN-23017-CPD-25493/CYS//CPD-25494/L-GAMMA-GLUTAMYLCYSTEINE.50. BioCyc RXN-23017-CPD-25493/L-ALPHA-ALANINE//CPD-25494/CPD-22081.47. BioCyc RXN-6601-CYS/GLUTATHIONE//L-GAMMA-GLUTAMYLCYSTEINE/CYS-GLY.50. BioCyc RXN-6601-L-ALPHA-ALANINE/GLUTATHIONE//CPD-22081/CYS-GLY.47. BioCyc RXN-9157 BioCyc RXN66-336-LEUKOTRIENE-C4/CYS//L-GAMMA-GLUTAMYLCYSTEINE/CPD66-21.54. BioCyc RXN66-336-LEUKOTRIENE-C4/L-ALPHA-ALANINE//CPD-22081/CPD66-21.51.