Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA3809
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: fdx2
Status: annotated
Amino acids: 112
Structure source: ColabFold

GO

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:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. GO:0140647 A electron transport chain in which one or more electron carriers operate to transfer electrons from donors to a cytochrome P450 protein or domain. Electron carriers operating in this chain include FAD-containing flavoproteins or domains, FMN domains, ferredoxins and cytochrome b5. The reduced cytochrome P450 functions as the terminal oxidase and participates in a wide range of biochemical pathways.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 46.316
Human E-value: 2.16e-17
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

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 0.63

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4

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:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0140647 A electron transport chain in which one or more electron carriers operate to transfer electrons from donors to a cytochrome P450 protein or domain. Electron carriers operating in this chain include FAD-containing flavoproteins or domains, FMN domains, ferredoxins and cytochrome b5. The reduced cytochrome P450 functions as the terminal oxidase and participates in a wide range of biochemical pathways.

Sequence Features

Domain/signature hits from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
42	52	ProSitePatterns	PS00814	Adrenodoxin family, iron-sulfur binding region signature.
42	52	InterPro	IPR018298	Adrenodoxin, iron-sulphur binding site
13	91	Pfam	PF00111	2Fe-2S iron-sulfur cluster binding domain
13	91	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
18	108	PANTHER	PTHR23426	FERREDOXIN/ADRENODOXIN
18	108	InterPro	IPR001055	Adrenodoxin
1	112	Gene3D	G3DSA:3.10.20.30	-
1	112	InterPro	IPR012675	Beta-grasp domain superfamily
42	52	PRINTS	PR00355	Adrenodoxin signature
42	52	InterPro	IPR001055	Adrenodoxin
60	74	PRINTS	PR00355	Adrenodoxin signature
60	74	InterPro	IPR001055	Adrenodoxin
83	91	PRINTS	PR00355	Adrenodoxin signature
83	91	InterPro	IPR001055	Adrenodoxin
4	106	SUPERFAMILY	SSF54292	2Fe-2S ferredoxin-like
4	106	InterPro	IPR036010	2Fe-2S ferredoxin-like superfamily
2	104	ProSiteProfiles	PS51085	2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
2	104	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
2	110	NCBIfam	TIGR02007	ferredoxin, 2Fe-2S type, ISC system
2	110	InterPro	IPR011536	Ferredoxin 2Fe-2S type, proteobacteria
14	99	CDD	cd00207	fer2
14	99	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain

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
ColabFold PA3809	ColabFold	—	—	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				0.63

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.

1 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
FES	1I7H	P0A9R4	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`

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.

PA3809