Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA2783
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA2783 mep72
Status: annotated
Amino acids: 599
Structure source: AlphaFold

EC

3.4.24.33

GO

GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures. GO:0005615 OBSOLETE. That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. GO:0019867 The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites. GO:0004175 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. GO:0016798 Catalysis of the hydrolysis of any glycosyl bond. GO:0046872 Binding to a metal ion.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
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 0.325

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

3.4.24.33

Gene Ontology (GO)

8

GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures.
GO:0005615 OBSOLETE. That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
GO:0019867 The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites.
GO:0004175 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
GO:0016798 Catalysis of the hydrolysis of any glycosyl bond.
GO:0046872 Binding to a metal ion.
GO:0008237 Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
GO:0097264 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds.

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
292	443	Gene3D	G3DSA:2.60.120.260	-
1	20	SignalP_EUK	SignalP-noTM	SignalP-noTM
306	440	SUPERFAMILY	SSF49785	Galactose-binding domain-like
306	440	InterPro	IPR008979	Galactose-binding-like domain superfamily
21	599	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
16	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
46	175	Pfam	PF13582	Metallo-peptidase family M12B Reprolysin-like
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
458	583	Pfam	PF02018	Carbohydrate binding domain
458	583	InterPro	IPR003305	Carbohydrate-binding, CenC-like
22	220	SUPERFAMILY	SSF55486	Metalloproteases ("zincins"), catalytic domain
1	20	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
8	199	FunFam	G3DSA:3.40.390.10:FF:000149	Carbohydrate-binding protein
456	599	Gene3D	G3DSA:2.60.120.260	-
8	199	Gene3D	G3DSA:3.40.390.10	Collagenase (Catalytic Domain)
8	199	InterPro	IPR024079	Metallopeptidase, catalytic domain superfamily
455	598	SUPERFAMILY	SSF49785	Galactose-binding domain-like
455	598	InterPro	IPR008979	Galactose-binding-like domain superfamily
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region
4	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.

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 PA2783	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				0.325
3				0.248

PA2783