Protein profile

PA2466

ferrioxamine receptor FoxA

Genome: NC_002516.2

Gene: foxA PA2466 Structure source: Experimental + AlphaFold UniProt Q9I116
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Amino acids 820
Annotations 10
Features 26
PDB binders 8
Druggability 0.523

Overview

Basic information about this protein and its source genome.

Accession
PA2466
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
foxA PA2466
Status
annotated
Amino acids
820
Structure source
Experimental + AlphaFold
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:0019867 The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites. GO:0015344 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: siderophore-iron(ferrioxamine)(out) + H+(out) = siderophore-iron(ferrioxamine)(in) + H+(in). GO:0038023 Receiving a signal and transmitting it in the cell to initiate a change in cell activity. A signal is a physical entity or change in state that is used to transfer information in order to trigger a response. GO:0007166 The series of molecular signals initiated by an extracellular ligand binding to a receptor located on the cell surface. The pathway ends with regulation of a downstream cellular process, e.g. transcription. GO:0015675 The directed movement of nickel (Ni) cations into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

Target profile

Computed evidence for target prioritization.

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

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 0.523
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

10 GO

Gene Ontology (GO)

10
  • 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:0019867 The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites.
  • GO:0015344 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: siderophore-iron(ferrioxamine)(out) + H+(out) = siderophore-iron(ferrioxamine)(in) + H+(in).
  • GO:0038023 Receiving a signal and transmitting it in the cell to initiate a change in cell activity. A signal is a physical entity or change in state that is used to transfer information in order to trigger a response.
  • GO:0007166 The series of molecular signals initiated by an extracellular ligand binding to a receptor located on the cell surface. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
  • GO:0015675 The directed movement of nickel (Ni) cations into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0015891 The directed movement of siderophores, low molecular weight Fe(III)-chelating substances, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0033214 A process in which iron (Fe3+) is solubilized by ferric iron-specific chelators, known as siderophores is imported into the cell by transmembrane transport or endocytosis.
  • GO:0006829 The directed movement of zinc (Zn II) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0015343 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: siderophore-iron(out) + H+(out) = siderophore-iron(in) + H+(in).

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records
Show feature table
Start End DB Term Name
48 820 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
48 149 Gene3D G3DSA:3.55.50.30 -
29 40 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
129 820 PANTHER PTHR32552 FERRICHROME IRON RECEPTOR-RELATED
129 820 InterPro IPR039426 TonB-dependent receptor-like
1 40 SignalP_GRAM_NEGATIVE SignalP-noTM SignalP-noTM
356 819 Pfam PF00593 TonB dependent receptor
356 819 InterPro IPR000531 TonB-dependent receptor-like, beta-barrel
291 820 Gene3D G3DSA:2.40.170.20 -
291 820 InterPro IPR036942 TonB-dependent receptor-like, beta-barrel domain superfamily
1 47 SignalP_GRAM_POSITIVE SignalP-TM SignalP-TM
174 820 NCBIfam TIGR01783 TonB-dependent siderophore receptor
174 820 InterPro IPR010105 TonB-dependent siderophore receptor
178 820 CDD cd01347 ligand_gated_channel
173 277 Pfam PF07715 TonB-dependent Receptor Plug Domain
173 277 InterPro IPR012910 TonB-dependent receptor, plug domain
1 28 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
155 287 Gene3D G3DSA:2.170.130.10 -
155 287 InterPro IPR037066 TonB-dependent receptor, plug domain superfamily
78 129 SMART SM00965 STN_2
78 129 InterPro IPR011662 Secretin/TonB, short N-terminal domain
41 47 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
288 820 FunFam G3DSA:2.40.170.20:FF:000005 TonB-dependent siderophore receptor
1 47 Phobius SIGNAL_PEPTIDE Signal peptide region
135 820 SUPERFAMILY SSF56935 Porins
155 288 FunFam G3DSA:2.170.130.10:FF:000001 Catecholate siderophore TonB-dependent receptor

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

6 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
PDB 6Z8A
X-ray 2.95 Å A
94.6% 45-820
PDBe RCSB PDBj File
Viewing
PDB 6I97
X-ray 3.35 Å A,B
93.7% 53-820
PDBe RCSB PDBj File
Loaded
PDB 6I96
X-ray 1.85 Å A
82.6% 144-820
PDBe RCSB PDBj File
Loaded
PDB 6I98
X-ray 2.80 Å A
82.6% 144-820
PDBe RCSB PDBj File
Loaded
PDB 8RM3
X-ray 2.22 Å A
100.0% 1-820
PDBe RCSB PDBj File
Metadata only
PDB 8RMI
X-ray 2.48 Å A
100.0% 1-820
PDBe RCSB PDBj File
Metadata only
AlphaFold PA2466
AlphaFold — — full sequence — Loaded
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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.

58 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.

Show only:
Ligand Source crystal MW · LogP · TPSA Lipinski PAINS SMILES
6L0
6Z8A 2.95 Å Open crystal
598.7 Da LogP 0.63 TPSA 208.9 2 viol. ✓ Clean C1CCNC(=O)CCC(=O)N(CCCCCNC(=O)CCC(=O)N(C/C=C/CC…
C8E
6I98 2.80 Å Open crystal
306.4 Da LogP 2.41 TPSA 57.2 ✓ Ro5 ✓ Clean CCCCCCCCOCCOCCOCCOCCO
FTT
6I98 2.80 Å Open crystal
244.4 Da LogP 3.74 TPSA 57.5 ✓ Ro5 ✓ Clean CCCCCCCCCCC[C@H](CC(=O)O)O

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.