Protein profile

PA5203

glutamate--cysteine ligase

Genome: NC_002516.2

Gene: gshA PA5203 Structure source: AlphaFold UniProt Q9HTY6
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Amino acids 527
Annotations 7
Features 17
PDB binders 3
Druggability 0.77

Overview

Basic information about this protein and its source genome.

Accession
PA5203
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
gshA PA5203
Status
annotated
Amino acids
527
Structure source
AlphaFold
EC
6.3.2.2
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0004357 Catalysis of the reaction: L-cysteine + L-glutamate + ATP = L-gamma-glutamyl-L-cysteine + ADP + 2 H+ + phosphate. GO:0046872 Binding to a metal ion. 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. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.77
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MSDLLSRRLALLGAAANLPLLTECLHGIERECLRVDSDGKLALTPHPRALGSTLTHPQITTDYSEALLEFITPTETDVADTLGDLERIHRFASSKLDGEYLWSPSMPCELPDEESIPIARYGSSMIGRLKYVYRKGLALRYGKTMQCIAGIHYNFSLPERLWPLLRQAEGSELSERDYQSAAYIALIRNFRRYSWLLMYLFGASPALDAGFLRGRPSQLERLDEHTLYLPYATSLRMSDLGYQNNAQAGLTPCYNDLQSYIDSLRQAVSTPYPPYEKVGTKQDGEWVQLNTNILQIENEYYSSIRPKRVTYTGERPVQALAARGVQYVEVRCLDINPFLPLGIDLDEARFLDAFLLFCAFSDSPLLNGECSDATDNFLAVVKEGRRPGLQLQRRGQPVELQVWANELLERIADTAALLDRARGGEAHAAALAAQRAKVADAELTPSAQVLKVMRERGESFEAFSLRQSREHAEYFRQHPLAAEEQARFEKMASDSLAEQTELERDQDGDFDTFVAAYQASILGLISN

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0004357 Catalysis of the reaction: L-cysteine + L-glutamate + ATP = L-gamma-glutamyl-L-cysteine + ADP + 2 H+ + phosphate.
  • GO:0046872 Binding to a metal ion.
  • 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.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records
Show feature table
Start End DB Term Name
10 378 InterPro IPR007370 Glutamate--cysteine ligase
9 16 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
25 527 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
8 514 SUPERFAMILY SSF55931 Glutamine synthetase/guanido kinase
8 514 InterPro IPR014746 Glutamine synthetase/guanido kinase, catalytic domain
17 24 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
6 517 NCBIfam TIGR01434 glutamate--cysteine ligase
6 517 InterPro IPR006334 Glutamate--cysteine ligase, monofunctional
21 523 Gene3D G3DSA:3.30.590.20 -
1 527 Hamap MF_00578 Glutamate--cysteine ligase [gshA].
1 527 InterPro IPR006334 Glutamate--cysteine ligase, monofunctional
21 523 FunFam G3DSA:3.30.590.20:FF:000007 Glutamate--cysteine ligase
1 24 Phobius SIGNAL_PEPTIDE Signal peptide region
1 8 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
10 378 Pfam PF04262 Glutamate-cysteine ligase
1 520 PANTHER PTHR38761 GLUTAMATE--CYSTEINE LIGASE
1 520 InterPro IPR006334 Glutamate--cysteine ligase, monofunctional

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA5203
AlphaFold — — full sequence — Viewing
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
2 0.77
1 0.557
4 0.421
8 0.226

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.

53 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
AF3
2D33
P0A6W9 84.0 Da LogP 0.88 TPSA 0.0 ✓ Ro5 ✓ Clean F[Al](F)F
ANP
2D32
P0A6W9 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)…
P2S
1VA6
P0A6W9 346.3 Da LogP -0.54 TPSA 187.6 ✓ Ro5 ✓ Clean CC[C@H](C[S@](=NP(=O)(O)O)(=O)CC[C@@H](C(=O)O)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.