Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA5047
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA5047
Status: annotated
Amino acids: 479
Structure source: AlphaFold

GO

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0046872 Binding to a metal ion. GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain 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: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:0051603 OBSOLETE. The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells. GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 24.514
Human E-value: 3.74e-11
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 0.858

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0046872 Binding to a metal ion.
GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain 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: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:0051603 OBSOLETE. The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Sequence Features

Domain/signature hits from InterPro and related databases.

14 records

Show feature table

Start	End	DB	Term	Name
37	249	CDD	cd07333	M48C_bepA_like
51	140	FunFam	G3DSA:3.30.2010.10:FF:000014	Peptidase M48 Ste24p
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
51	140	Gene3D	G3DSA:3.30.2010.10	Metalloproteases ("zincins"), catalytic domain
5	24	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
61	249	Pfam	PF01435	Peptidase family M48
61	249	InterPro	IPR001915	Peptidase M48
1	19	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
1	23	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	20	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
16	23	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
24	479	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
5	257	PANTHER	PTHR22726	METALLOENDOPEPTIDASE OMA1
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...

Legend High Medium Low

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 PA5047	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
5				0.858
15				0.336
1				0.236

PA5047