KpATCC43816 Protein target profile

glutamine synthetase, type I

Accession: VK055_3295

Gene: AIK81856.1 glnA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GG67

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Length 469

Pocket druggability (P2Rank · AlphaFold DB model) 0.806

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 62 total records

Functional annotation 1 EC 9 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

No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Moderate predicted binding pocket FPocket selected-pocket score 0.62. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.81. 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 (%): 27.548 Lower values reduce human off-target concern.
Human E-value: 1.8e-12
Gut microbiome similarity: 8.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 95.736 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.34 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) 0.806

Structure A0A0H3GG67

Pocket Pocket 1

Druggability (FPocket) 0.619

Structure A0A0H3GG67

Pocket Pocket 1

ColabFold model

P2Rank 0.808 · Pocket 1

FPocket 0.534 · Pocket 20

Core conservation Accessory gene

Roary accessory

CoreCruncher core

Gut microbiome 413 / 4744 genomes with a hit

Prevalence 8.7%

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.

MSAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPSHQVNAEFFEEGKMFDGSSIGGWKGINESDMVLMPDASTAVIDPFYEEPTLIIRCDILEPGTLQGYDRDPRSIAKRAEEYLRATGIADTVLFGPEPEFFLFDDIRFGASISGSHVAIDDIEGAWNSSTKYEGGNKGHRPGVKGGYFPVPPVDSSQDIRSTMCMIMEEMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFGKTATFMPKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALFYIGGVIKHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVTSPKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEAMDKNLYDLPPEEAKEIPQVAGSLEEALQALDADREFLTAGGVFTNDAIDAYIALRMEENDRVRMTPHPVEFELYYSV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

6.3.1.2

Gene Ontology (GO)

GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0004356 Catalysis of the reaction: ATP + L-glutamate + NH4+ = ADP + H+ + L-glutamine + phosphate.
GO:0006807 OBSOLETE. The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.
GO:0006542 OBSOLETE. The chemical reactions and pathways resulting in the formation of glutamine, 2-amino-4-carbamoylbutanoic acid.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0046872 Binding to a metal ion.
GO:0019740 A series of processes that forms an integrated mechanism by which a cell or an organism detects the depletion of primary nitrogen source, usually ammonia, and then activates genes to scavenge the last traces of the primary nitrogen source and to transport and metabolize alternative nitrogen sources. The utilization process begins when the cell or organism detects nitrogen levels, includes the activation of genes whose products detect, transport or metabolize nitrogen-containing substances, and ends when nitrogen is incorporated into the cell or organism's metabolism.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
102	379	SMART	SM01230	Gln_synt_C_2
102	379	InterPro	IPR008146	Glutamine synthetase, catalytic domain
2	468	PANTHER	PTHR43407	GLUTAMINE SYNTHETASE
386	398	ProSitePatterns	PS00182	Glutamine synthetase class-I adenylation site.
386	398	InterPro	IPR001637	Glutamine synthetase class-I, adenylation site
102	468	SUPERFAMILY	SSF55931	Glutamine synthetase/guanido kinase
102	468	InterPro	IPR014746	Glutamine synthetase/guanido kinase, catalytic domain
259	274	ProSitePatterns	PS00181	Glutamine synthetase putative ATP-binding region signature.
259	274	InterPro	IPR027303	Glutamine synthetase, glycine-rich site
105	457	FunFam	G3DSA:3.30.590.10:FF:000001	Glutamine synthetase
50	68	ProSitePatterns	PS00180	Glutamine synthetase signature 1.
50	68	InterPro	IPR027302	Glutamine synthetase, N-terminal conserved site
105	457	Gene3D	G3DSA:3.30.590.10	Glutamine synthetase/guanido kinase, catalytic domain
13	97	ProSiteProfiles	PS51986	Glutamine synthetase (GS) beta-grasp domain profile.
13	97	InterPro	IPR008147	Glutamine synthetase, N-terminal domain
105	469	ProSiteProfiles	PS51987	Glutamine synthetase (GS) catalytic domain profile.
105	469	InterPro	IPR008146	Glutamine synthetase, catalytic domain
3	99	SUPERFAMILY	SSF54368	Glutamine synthetase, N-terminal domain
3	99	InterPro	IPR036651	Glutamine synthetase, N-terminal domain superfamily
14	95	Pfam	PF03951	Glutamine synthetase, beta-Grasp domain
14	95	InterPro	IPR008147	Glutamine synthetase, N-terminal domain
1	103	Gene3D	G3DSA:3.10.20.70	-
1	103	InterPro	IPR036651	Glutamine synthetase, N-terminal domain superfamily
4	468	NCBIfam	TIGR00653	glutamine synthetase, type I
4	468	InterPro	IPR004809	Glutamine synthetase type I
103	466	Pfam	PF00120	Glutamine synthetase, catalytic domain
103	466	InterPro	IPR008146	Glutamine synthetase, catalytic domain
1	104	FunFam	G3DSA:3.10.20.70:FF:000001	Glutamine synthetase

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

0.806

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Surrounding area

Pocket 2 P2Rank #2

0.361

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Surrounding area

Pocket 3 P2Rank #3

0.169

Likely same site as FPocket 3 1.0 Å 13 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.082

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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

0.619

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Surrounding area

Pocket 2 FPocket #3

0.521

Likely same site as P2Rank 3 1.0 Å 13 shared residues 100% of smaller site

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Surrounding area

Pocket 3 FPocket #15

0.304

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Surrounding area

Pocket 4 FPocket #6

0.203

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Surrounding area

Residue sets

UniProt: Binding site:130-130

UniProt: Binding site:132-132

UniProt: Binding site:208-208

UniProt: Binding site:213-213

UniProt: Binding site:221-221

UniProt: Binding site:265-266

UniProt: Binding site:270-270

UniProt: Binding site:272-274

UniProt: Binding site:322-322

UniProt: Binding site:328-328

UniProt: Binding site:340-340

UniProt: Binding site:353-353

UniProt: Binding site:358-358

UniProt: Binding site:360-360

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.808

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Surrounding area

Pocket 2 P2Rank #2

0.195

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Surrounding area

Pocket 3 P2Rank #3

0.128

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Surrounding area

Pocket 4 P2Rank #4

0.114

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Surrounding area

Pocket 5 P2Rank #5

0.034

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Surrounding area

Residue sets

UniProt: Binding site:130-130

UniProt: Binding site:132-132

UniProt: Binding site:208-208

UniProt: Binding site:213-213

UniProt: Binding site:221-221

UniProt: Binding site:265-266

UniProt: Binding site:270-270

UniProt: Binding site:272-274

UniProt: Binding site:322-322

UniProt: Binding site:328-328

UniProt: Binding site:340-340

UniProt: Binding site:353-353

UniProt: Binding site:358-358

UniProt: Binding site:360-360

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_A0A0H3GG67	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3295	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 and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 12 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1AZ PDB via homolog 424.3 Da · LogP 1.63 · TPSA 74.3 Open detail RCSB PDB

2K9 PDB via homolog Detail RCSB PDB

46B PDB via homolog Detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

IQ1 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
1AZ RCSB PDB	2WGS	P9WN39	424.3 Da LogP 1.63 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c2c(nc1N3CCOCC3)N(C(=O)N(C2=O)Cc4ccc(c(c4)Cl…`
2K9 RCSB PDB	4XYC	P9WN38	297.3 Da LogP 2.28 TPSA 47.3	✓ Ro5	✓ Clean	`c1ccc(cc1)c2cccc3c2C=C4C3=NC(=O)c5n4ccn5`
46B RCSB PDB	4ACF	P9WN39	418.3 Da LogP 4.44 TPSA 75.9	✓ Ro5	✓ Clean	`CCCCNc1c(nc2n1cc(cc2)Br)c3ccc(cc3)OCC(=O)O`
ANP RCSB PDB	3NG0	P77961	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
IQ1 RCSB PDB	3ZXR	P9WN39	328.4 Da LogP 4.98 TPSA 54.5	✓ Ro5	✓ Clean	`CC(C)(C)c1[nH]c(c(n1)c2cc3ccccc3nc2)c4ccncc4`
MXI RCSB PDB	3ZXV	P9WN39	372.5 Da LogP 5.18 TPSA 76.8	1 viol.	✓ Clean	`CC(C)(C)c1[nH]c(c(n1)c2ccc3cc(ccc3c2)OC)c4ccnc(…`
P3P RCSB PDB	5ZLP	P94845	261.1 Da LogP -0.19 TPSA 147.2	✓ Ro5	✓ Clean	`C[P@](=O)(CC[C@@H](C(=O)O)N)OP(=O)(O)O`
P3S RCSB PDB	4LNI	P12425	260.2 Da LogP -1.02 TPSA 150.3	✓ Ro5	✓ Clean	`C[S@](=NP(=O)(O)O)(=O)CC[C@@H](C(=O)O)N`
PPQ RCSB PDB	1FPY	P0A1P6	181.1 Da LogP -0.31 TPSA 100.6	✓ Ro5	✓ Clean	`C[P@](=O)(CC[C@@H](C(=O)O)N)O`
TL RCSB PDB	1F1H	P0A1P6	204.4 Da LogP -0.38 TPSA 0.0	✓ Ro5	✓ Clean	`[Tl+]`

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
CHEMBL3215977 ChEMBL	P0A9C5	6.23 ~588.8 nM	269.1 Da LogP -0.18 TPSA 126.6	✓ Ro5	✓ Clean	`Cl.Cl.NCP(=O)(O)CC[C@H](N)C(=O)O`
CHEMBL535153 ChEMBL	P0A9C5	6.22 ~602.6 nM	217.6 Da LogP 0.11 TPSA 100.6	✓ Ro5	✓ Clean	`CP(=O)(O)CC[C@H](N)C(=O)O.Cl`

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
ZINC1094334 ZINC	0.843	389.8 Da LogP 0.97 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(N2CCOCC2)nc2c1c(=O)n(Cc1ccc(Cl)cc1)c(=O)n2C`
ZINC8916385 ZINC	0.827	422.3 Da LogP 2.78 TPSA 65.1	✓ Ro5	✓ Clean	`Cn1c(N2CCCCC2)nc2c1c(=O)n(Cc1ccc(Cl)c(Cl)c1)c(=…`
ZINC1094329 ZINC	0.811	436.3 Da LogP 3.03 TPSA 65.1	✓ Ro5	✓ Clean	`CC1CCN(c2nc3c(c(=O)n(Cc4ccc(Cl)c(Cl)c4)c(=O)n3C…`
ZINC12360002 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC7425789 ZINC	0.808	369.4 Da LogP 0.63 TPSA 74.3	✓ Ro5	✓ Clean	`Cc1ccc(Cn2c(=O)c3c(nc(N4CCOCC4)n3C)n(C)c2=O)cc1`
ZINC13388673 ZINC	0.804	355.4 Da LogP 0.32 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(N2CCOCC2)nc2c1c(=O)n(Cc1ccccc1)c(=O)n2C`
ZINC1127306 ZINC	0.792	373.4 Da LogP 0.46 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(N2CCOCC2)nc2c1c(=O)n(Cc1ccc(F)cc1)c(=O)n2C`
ZINC6444971 ZINC	0.792	434.3 Da LogP 1.08 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(N2CCOCC2)nc2c1c(=O)n(Cc1ccc(Br)cc1)c(=O)n2C`
ZINC8926317 ZINC	0.792	424.3 Da LogP 1.63 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(=O)c2c(nc(N3CCOCC3)n2Cc2ccc(Cl)c(Cl)c2)n(C…`
ZINC13115750 ZINC	0.750	452.3 Da LogP 2.40 TPSA 74.3	✓ Ro5	✓ Clean	`C[C@H]1CN(c2nc3c(c(=O)n(Cc4ccc(Cl)c(Cl)c4)c(=O)…`
ZINC2265176 ZINC	0.750	452.3 Da LogP 2.40 TPSA 74.3	✓ Ro5	✓ Clean	`C[C@@H]1CN(c2nc3c(c(=O)n(Cc4ccc(Cl)c(Cl)c4)c(=O…`
ZINC38154058 ZINC	0.750	452.3 Da LogP 2.40 TPSA 74.3	✓ Ro5	✓ Clean	`C[C@H]1CN(c2nc3c(c(=O)n(Cc4ccc(Cl)c(Cl)c4)c(=O)…`
ZINC13518964 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC9324586 ZINC	0.741	465.3 Da LogP 1.49 TPSA 108.2	✓ Ro5	✓ Clean	`Cn1c(N2CCC(C(N)=O)CC2)nc2c1c(=O)n(Cc1ccc(Cl)c(C…`
ZINC1127852 ZINC	0.737	424.3 Da LogP 1.63 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(N2CCOCC2)nc2c1c(=O)n(Cc1ccc(Cl)cc1Cl)c(=O)…`
ZINC1133233 ZINC	0.736	431.5 Da LogP 1.83 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(=O)n(Cc2ccccc2)c(=O)c2c1nc(N1CCOCC1)n2Cc1c…`
ZINC1277814 ZINC	0.732	389.8 Da LogP 0.97 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(N2CCOCC2)nc2c1c(=O)n(Cc1ccccc1Cl)c(=O)n2C`
ZINC4096224 ZINC	0.729	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423 ZINC	0.703	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC23115420 ZINC	0.702	383.5 Da LogP 1.36 TPSA 74.3	✓ Ro5	✓ Clean	`CC(C)n1c(N2CCOCC2)nc2c1c(=O)n(Cc1ccccc1)c(=O)n2C`

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.

glutamine synthetase, type I

Promising target candidate with multiple supporting evidence streams.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways