Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA2416
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: treA PA2416
Status: annotated
Amino acids: 545
Structure source: AlphaFold

EC

3.2.1.28

GO

GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). GO:0004555 Catalysis of the reaction: alpha,alpha-trehalose + H2O = 2 D-glucose. GO:0015927 Catalysis of the hydrolysis of trehalose or a trehalose derivative. GO:0071474 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell. GO:0005993 The chemical reactions and pathways resulting in the breakdown of trehalose, a disaccharide that consists of two molecules of glucose and is isomeric with sucrose. GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 35.294
Human E-value: 5.4900000000000005e-77
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Periplasmic

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 0.563

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MPDRTALPRAMLAAWVLLLLAACSQGPAPTPPASWGWQDASGERAIAPDEAYPELFQAVQENRLFSDQKHFVDALPLREPARIRADYLRERERPGFDLRAFVGRNFEESGSVETAPPEAGADLASHISDLWPALTRHYEQVPAHSSLLPLPKPYVVPGGRFREVYYWDSYFTMLGLAESGQHQRVRDMLDNFAYLIDTYGHIPNGNRSYYLSRSQPPFFAYMVDLQARREGDAAYRRYLPQLQKEYAYWMEGSAGLRPNEARLHVVKLADGSLLNRYWDNRDTPRQESFLEDRATAARAPQRPAGEVYRDLRAGAESGWDFSSRWLDDGRELASIRTTAIVPVDLNALLYHLERIIAKACASSALKACEQGYGARAEKRRQAIEDHLWHPAGYYADYDWQRRRPIERINAASLFPLFTGLASAERAGRTADSVAAQLLRPGGLATTTRASGQQWDEPNGWAPLQWVAVQGLRAYGRDALAEDIGRRFLAQVQQVYDREGKLVEKYDISGNQGGGGGGEYPLQDGFGWSNGVTLQLLRLYGPGAGR

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

3.2.1.28

Gene Ontology (GO)

7

GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
GO:0004555 Catalysis of the reaction: alpha,alpha-trehalose + H2O = 2 D-glucose.
GO:0015927 Catalysis of the hydrolysis of trehalose or a trehalose derivative.
GO:0071474 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell.
GO:0005993 The chemical reactions and pathways resulting in the breakdown of trehalose, a disaccharide that consists of two molecules of glucose and is isomeric with sucrose.
GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
GO:0005991 The chemical reactions and pathways involving trehalose, a disaccharide that consists of two molecules of glucose and is isomeric with sucrose.

Sequence Features

Domain/signature hits from InterPro and related databases.

36 records

Show feature table

Start	End	DB	Term	Name
1	32	Phobius	SIGNAL_PEPTIDE	Signal peptide region
2	541	Hamap	MF_01060	Periplasmic trehalase [treA].
2	541	InterPro	IPR023720	Trehalase, periplasmic
33	545	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
52	540	PANTHER	PTHR23403	TREHALASE
52	540	InterPro	IPR001661	Glycoside hydrolase, family 37
49	542	SUPERFAMILY	SSF48208	Six-hairpin glycosidases
49	542	InterPro	IPR008928	Six-hairpin glycosidase superfamily
24	32	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	21	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
1	26	SignalP_EUK	SignalP-noTM	SignalP-noTM
157	170	ProSitePatterns	PS00927	Trehalase signature 1.
157	170	InterPro	IPR018232	Glycoside hydrolase, family 37, conserved site
64	540	Pfam	PF01204	Trehalase
64	540	InterPro	IPR001661	Glycoside hydrolase, family 37
1	23	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
453	462	ProSitePatterns	PS00928	Trehalase signature 2.
453	462	InterPro	IPR018232	Glycoside hydrolase, family 37, conserved site
1	11	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
199	217	PRINTS	PR00744	Glycosyl hydrolase family 37 signature
199	217	InterPro	IPR001661	Glycoside hydrolase, family 37
274	291	PRINTS	PR00744	Glycosyl hydrolase family 37 signature
274	291	InterPro	IPR001661	Glycoside hydrolase, family 37
523	536	PRINTS	PR00744	Glycosyl hydrolase family 37 signature
523	536	InterPro	IPR001661	Glycoside hydrolase, family 37
446	462	PRINTS	PR00744	Glycosyl hydrolase family 37 signature
446	462	InterPro	IPR001661	Glycoside hydrolase, family 37
340	357	PRINTS	PR00744	Glycosyl hydrolase family 37 signature
340	357	InterPro	IPR001661	Glycoside hydrolase, family 37
308	325	PRINTS	PR00744	Glycosyl hydrolase family 37 signature
308	325	InterPro	IPR001661	Glycoside hydrolase, family 37
46	542	FunFam	G3DSA:1.50.10.10:FF:000003	Cytoplasmic trehalase
46	543	Gene3D	G3DSA:1.50.10.10	-
46	543	InterPro	IPR012341	Six-hairpin glycosidase-like superfamily
12	23	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	33	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM

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...

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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 PA2416	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
9				0.404
8				0.304
2				0.244

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.

11 records

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
3CU	2JJB	P13482	205.2 Da LogP -3.51 TPSA 104.4	✓ Ro5	✓ Clean	`C1[C@@H]([C@H]([C@H]2[N@@]1[C@@H]([C@H]([C@@H]2…`

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
VDM	O70282	8.31	335.4 Da LogP -4.58 TPSA 173.9	1 viol.	✓ Clean	`C1[C@@H]([C@H]([C@@H]([C@H]([C@H]1N[C@H]2C=C([C…`
CHEMBL2270892	P32358	7.31	366.3 Da LogP -6.04 TPSA 204.7	2 viol.	✓ Clean	`OC[C@H]1O[C@H](NC2=N[C@@H]3[C@H](O2)[C@@H](O)[C…`
CHEMBL145196	O43280	6.75	321.3 Da LogP -4.56 TPSA 162.9	1 viol.	✓ Clean	`OCC1=CC(NC2COC(CO)C(O)C2O)C(O)C(O)C1O`

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
ZINC1857787936	0.647	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@@H](N[C@@H]2C[C@@H](CO)[C@H](O[C@H]3O[…`
ZINC2053528368	0.647	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…`
ZINC2053528371	0.647	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…`
ZINC2053528373	0.647	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…`
ZINC2053528375	0.647	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…`
ZINC8437016	0.647	497.5 Da LogP -6.75 TPSA 253.0	2 viol.	✓ Clean	`OCC1=C[C@H](N[C@H]2C[C@H](CO)[C@@H](O[C@@H]3O[C…`
ZINC16052241	0.600	335.4 Da LogP -4.58 TPSA 173.9	1 viol.	✓ Clean	`OCC1=C[C@H](N[C@H]2C[C@H](CO)[C@@H](O)[C@H](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.

PA2416