Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA4691
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4691 msrQ
Status: annotated
Amino acids: 202
Structure source: AlphaFold

GO

GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways. GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. GO:0046872 Binding to a metal ion. GO:0016679 Catalysis of an oxidation-reduction (redox) reaction in which a diphenol or related substance acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: CytoplasmicMembrane

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 0.896

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

7

GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0046872 Binding to a metal ion.
GO:0016679 Catalysis of an oxidation-reduction (redox) reaction in which a diphenol or related substance acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0030091 The process of restoring a protein to its original state after damage by such things as oxidation or spontaneous decomposition of residues.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
112	134	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
98	108	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
170	188	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	4	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
165	169	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
3	199	PANTHER	PTHR36964	PROTEIN-METHIONINE-SULFOXIDE REDUCTASE HEME-BINDING SUBUNIT MSRQ
3	199	InterPro	IPR022837	Protein-methionine-sulfoxide reductase subunit MsrQ-like
190	202	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
64	74	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
5	23	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
24	42	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
75	97	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
147	165	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
43	63	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
170	189	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
43	154	Pfam	PF01794	Ferric reductase like transmembrane component
43	154	InterPro	IPR013130	Ferric reductase transmembrane component-like domain
5	27	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
37	54	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
147	164	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
109	127	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
128	146	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
75	97	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	195	Hamap	MF_01207	Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ [msrQ].
1	195	InterPro	IPR022837	Protein-methionine-sulfoxide reductase subunit MsrQ-like

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 PA4691	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				0.896
6				0.298
3				0.277

PA4691