Protein profile

PA5508

glutamine synthetase

Genome: NC_002516.2

Gene: PA5508 Structure source: Experimental + AlphaFold UniProt Q9HT65

Export view

Amino acids 443

Annotations 6

Features 15

PDB binders 9

Druggability 0.728

Overview

Basic information about this protein and its source genome.

Accession: PA5508
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA5508
Status: annotated
Amino acids: 443
Structure source: Experimental + AlphaFold

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0004356 Catalysis of the reaction: ATP + L-glutamate + NH4+ = ADP + H+ + L-glutamine + phosphate. GO:0046872 Binding to a metal ion. GO:0006542 OBSOLETE. The chemical reactions and pathways resulting in the formation of glutamine, 2-amino-4-carbamoylbutanoic acid. 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:0006807 OBSOLETE. The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 24.885
Human E-value: 4.7e-22
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 0.728

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MNRLQPVRLVSFVTTDLAGITRGRSLPLATLEEQLASGCGWVPANSSLTPQDLIDESSPWGSHGDLRLLPDPNSRVRVEQGPDAAAPALDYLHGNLVETDGTPWPACPRSLLRAEVERYRDSGLQVIAAFEHEFSLLGLPGERPAAAFSLQAQRAAGQFPGWLVSALAQAGTEPEMFLPEYGQRQYEVTCRPAQGVAAADRAVNVREVTREVARQMGLRTCFAPLPAPGAVTNGVHLHLSLQHADGSPLLYEPGRPNDLSELGEHWAAGVLAHLPALCALTAPTAASYLRLKPHHWSAAYACLGLRNREAALRICPVVSVGGKPLGKQYNLEFRPMDATTCPHLAMAAVLIAGRLGIERRLPLRALADVDPHGLSDEERQARGIQALPATLGDALDCLQRDEALCAELPKPLLDTYLAMKRHELALTAGLSDDDLCRHYAELY

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0004356 Catalysis of the reaction: ATP + L-glutamate + NH4+ = ADP + H+ + L-glutamine + phosphate.
GO:0046872 Binding to a metal ion.
GO:0006542 OBSOLETE. The chemical reactions and pathways resulting in the formation of glutamine, 2-amino-4-carbamoylbutanoic acid.
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:0006807 OBSOLETE. The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records

Show feature table

Start	End	DB	Term	Name
102	443	Gene3D	G3DSA:3.30.590.10	Glutamine synthetase/guanido kinase, catalytic domain
105	353	SMART	SM01230	Gln_synt_C_2
105	353	InterPro	IPR008146	Glutamine synthetase, catalytic domain
106	426	Pfam	PF00120	Glutamine synthetase, catalytic domain
106	426	InterPro	IPR008146	Glutamine synthetase, catalytic domain
3	104	Pfam	PF16952	Glutamine synthetase N-terminal domain
3	104	InterPro	IPR008147	Glutamine synthetase, N-terminal domain
102	443	FunFam	G3DSA:3.30.590.10:FF:000023	Probable glutamine synthetase
7	443	PANTHER	PTHR43785	GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE
1	101	Gene3D	G3DSA:3.10.20.70	-
1	101	InterPro	IPR036651	Glutamine synthetase, N-terminal domain superfamily
105	440	SUPERFAMILY	SSF55931	Glutamine synthetase/guanido kinase
105	440	InterPro	IPR014746	Glutamine synthetase/guanido kinase, catalytic domain
108	443	ProSiteProfiles	PS51987	Glutamine synthetase (GS) catalytic domain profile.
108	443	InterPro	IPR008146	Glutamine synthetase, catalytic domain

3D Structure

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

Loading 3D structure...

Legend High Medium Low

Structural evidence

1 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 4HPP	X-ray	2.50 Å	A	100.0% 1-443	PDBe RCSB PDBj File	Viewing
AlphaFold PA5508	AlphaFold	—	—	full sequence	—	Loaded

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
1				0.728
3				0.725
6				0.244

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	12.53	0.654
2	1.64	0.027
3	1.28	0.013
4	0.65	0.001

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				0.814
9				0.209

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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 59 via homologs

Structural ligands 9 0 loaded crystals

Bioactive compounds 0 50 ZINC candidates

Drug-like & clean 41 0 PAINS alerts

Best available ligand signal

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

1AZ PDB via homolog 2K9 PDB via homolog 46B PDB via homolog ANP PDB via homolog

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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	4XYC	P9WN38	297.3 Da LogP 2.28 TPSA 47.3	✓ Ro5	✓ Clean	`c1ccc(cc1)c2cccc3c2C=C4C3=NC(=O)c5n4ccn5`
46B	4ACF	P9WN39	418.3 Da LogP 4.44 TPSA 75.9	✓ Ro5	✓ Clean	`CCCCNc1c(nc2n1cc(cc2)Br)c3ccc(cc3)OCC(=O)O`
ANP	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	3ZXR	P9WN39	328.4 Da LogP 4.98 TPSA 54.5	✓ Ro5	✓ Clean	`CC(C)(C)c1[nH]c(c(n1)c2cc3ccccc3nc2)c4ccncc4`
MXI	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	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	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	5ZLP	P94845	181.1 Da LogP -0.31 TPSA 100.6	✓ Ro5	✓ Clean	`C[P@](=O)(CC[C@@H](C(=O)O)N)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
ZINC1094334	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	0.804	355.4 Da LogP 0.32 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(N2CCOCC2)nc2c1c(=O)n(Cc1ccccc1)c(=O)n2C`
ZINC1127306	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	0.737	424.3 Da LogP 1.63 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(N2CCOCC2)nc2c1c(=O)n(Cc1ccc(Cl)cc1Cl)c(=O)…`
ZINC1133233	0.736	431.5 Da LogP 1.83 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(=O)n(Cc2ccccc2)c(=O)c2c1nc(N1CCOCC1)n2Cc1c…`
ZINC1277814	0.732	389.8 Da LogP 0.97 TPSA 74.3	✓ Ro5	✓ Clean	`Cn1c(N2CCOCC2)nc2c1c(=O)n(Cc1ccccc1Cl)c(=O)n2C`
ZINC4096224	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	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	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	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	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	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	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	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	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	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	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.