Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA3185
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3185
Status: annotated
Amino acids: 283
Structure source: AlphaFold

EC

5.1.3.15

GO

GO:0030246 Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates. GO:0047938 Catalysis of the reaction: alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate. 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:0016853 Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. 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: Unknown

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 0.752

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MLEHPLQRFFHSMRAKRPFDWVRFQRRDLLLIDHPLCQAVFSRQGAQLLHFQPQGERPLLWCASEWPALSSAPVRGGIPVCWPWFGSHPNGSEWPQQGWARQREWRLLDAYADESKVVVSWQLDLEDWHVRLDARLGQRLELELCSYHEEDDDCLFSFALQPYWRVGALSRVVVHGMELESARGQRGASRIPGTWIPRGAVKQVLYHPGSLVLEDGGWNRRLRIDKNVSAGSVIWHPGSRPVEQVEPGEAERFLCIGAAGYRPGGLILAPGERMRLNLAAGLQ

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

5.1.3.15

Gene Ontology (GO)

5

GO:0030246 Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
GO:0047938 Catalysis of the reaction: alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate.
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:0016853 Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
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.

11 records

Show feature table

Start	End	DB	Term	Name
14	280	Gene3D	G3DSA:2.70.98.10	-
14	280	InterPro	IPR014718	Glycoside hydrolase-type carbohydrate-binding
3	283	PIRSF	PIRSF016020	PHexose_mutarotase
3	283	InterPro	IPR025532	Glucose-6-phosphate 1-epimerase
30	276	CDD	cd09020	D-hex-6-P-epi_like
30	276	InterPro	IPR025532	Glucose-6-phosphate 1-epimerase
18	277	SUPERFAMILY	SSF74650	Galactose mutarotase-like
18	277	InterPro	IPR011013	Galactose mutarotase-like domain superfamily
29	277	Pfam	PF01263	Aldose 1-epimerase
29	277	InterPro	IPR008183	Aldose 1-/Glucose-6-phosphate 1-epimerase
29	276	PANTHER	PTHR11122	APOSPORY-ASSOCIATED PROTEIN C-RELATED

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 PA3185	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
1				0.752
3				0.282

PA3185