Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA4692
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: msrP PA4692
Status: annotated
Amino acids: 337
Structure source: AlphaFold

EC

1.8.5.-

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:0046872 Binding to a metal ion. GO:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0016672 Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing group acts as a hydrogen or electron donor and reduces quinone or a related compound. GO:0030091 The process of restoring a protein to its original state after damage by such things as oxidation or spontaneous decomposition of residues.

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 0.745

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MLIKIPSRSDCSESEVTSETLYLSRRRLLGASFAGLALASGLPRLGFADEQRYAGVESVPAPGWFAEKLPQTRWQAVNVQGEAITPFKDATHYNNFYEFGPNKGDPAENASALKAEPWSVVIDGEVGKPGTYALEDFVKPYQLEERIYRLRCVEAWSMVIPWLGFPLADLLKRVEPNGQAKFVRFETLQRPEQMVGQRSGFSVIDWPYMEGLRMDEAMHPLAILAVGMYGRLLPNQNGAPLRLVVPWKYGFKSIKSIVRISLVREQPKTTWESIAANEYGFYANVNPQVDHPRWSQARERRLPSGLFSPNVRDTQMFNGYGSEVASLYSGMDLRKYY

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

1.8.5.-

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:0046872 Binding to a metal ion.
GO:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0016672 Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing group acts as a hydrogen or electron donor and reduces quinone or a related compound.
GO:0030091 The process of restoring a protein to its original state after damage by such things as oxidation or spontaneous decomposition of residues.
GO:0016667 Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Sequence Features

Domain/signature hits from InterPro and related databases.

9 records

Show feature table

Start	End	DB	Term	Name
114	271	Pfam	PF00174	Oxidoreductase molybdopterin binding domain
114	271	InterPro	IPR000572	Oxidoreductase, molybdopterin-binding domain
82	333	SUPERFAMILY	SSF56524	Oxidoreductase molybdopterin-binding domain
82	333	InterPro	IPR036374	Oxidoreductase, molybdopterin-binding domain superfamily
72	337	Gene3D	G3DSA:3.90.420.10	-
72	337	InterPro	IPR036374	Oxidoreductase, molybdopterin-binding domain superfamily
3	337	Hamap	MF_01206	Protein-methionine-sulfoxide reductase catalytic subunit MsrP [msrP].
3	337	InterPro	IPR022867	Protein-methionine-sulfoxide reductase subunit MsrP
70	333	PANTHER	PTHR43032	PROTEIN-METHIONINE-SULFOXIDE REDUCTASE

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 PA4692	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				0.745
8				0.397

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.

5 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
MO	1XDQ	P76342	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo]`
MSS	2BLF	Q9LA16	505.3 Da LogP -0.12 TPSA 188.9	3 viol.	✓ Clean	`C([C@@H]1C2=C([C@H]3[C@@H](O1)NC4=C(N3)C(=O)NC(…`
MTE	1XDY	P76342	395.4 Da LogP -0.54 TPSA 171.8	1 viol.	✓ Clean	`C([C@@H]1C(=C([C@H]2[C@@H](O1)NC3=C(N2)C(=O)NC(…`
O	1XDQ	P76342	18.0 Da LogP -0.82 TPSA 31.5	✓ Ro5	✓ Clean	`O`
W	1XDY	P76342	183.8 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[W+6]`

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).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

No virtual-screening candidates for this protein.

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.

PA4692