Protein profile

PA2398

ferripyoverdine receptor

Genome: NC_002516.2

Gene: PA2398 fpvA Structure source: Experimental + AlphaFold UniProt P48632
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Amino acids 815
Annotations 9
Features 28
PDB binders 8
Druggability 0.731

Overview

Basic information about this protein and its source genome.

Accession
PA2398
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2398 fpvA
Status
annotated
Amino acids
815
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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. 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:0002049 The chemical reactions and pathways resulting in the formation of the siderochrome pyoverdine. 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.

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 0.731
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MPAPHGLSPLSKAFLMRRAFQRRILPHSLAMALSLPLAGYVQAQEVEFDIPPQALGSALQEFGRQADIQVLYRPEEVRNKRSSAIKGKLEPNQAITELLRGTGASVDFQGNAITISVAEAADSSVDLGATMITSNQLGTITEDSGSYTPGTIATATRLVLTPRETPQSITVVTRQNMDDFGLNNIDDVMRHTPGITVSAYDTDRNNYYARGFSINNFQYDGIPSTARNVGYSAGNTLSDMAIYDRVEVLKGATGLLTGAGSLGATINLIRKKPTHEFKGHVELGAGSWDNYRSELDVSGPLTESGNVRGRAVAAYQDKHSFMDHYERKTSVYYGILEFDLNPDTMLTVGADYQDNDPKGSGWSGSFPLFDSQGNRNDVSRSFNNGAKWSSWEQYTRTVFANLEHNFANGWVGKVQLDHKINGYHAPLGAIMGDWPAPDNSAKIVAQKYTGETKSNSLDIYLTGPFQFLGREHELVVGTSASFSHWEGKSYWNLRNYDNTTDDFINWDGDIGKPDWGTPSQYIDDKTRQLGSYMTARFNVTDDLNLFLGGRVVDYRVTGLNPTIRESGRFIPYVGAVYDLNDTYSVYASYTDIFMPQDSWYRDSSNKLLEPDEGQNYEIGIKGEYLDGRLNTSLAYFEIHEENRAEEDALYNSKPTNPAITYAYKGIKAKTKGYEAEISGELAPGWQVQAGYTHKIIRDDSGKKVSTWEPQDQLSLYTSYKFKGALDKLTVGGGARWQGKSWQMVYNNPRSRWEKFSQEDYWLVDLMARYQITDKLSASVNVNNVFDKTYYTNIGFYTSASYGDPRNLMFSTRWDF

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Gene Ontology (GO)

9
  • 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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • 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:0002049 The chemical reactions and pathways resulting in the formation of the siderochrome pyoverdine.
  • 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:0019867 The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites.
  • 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.

28 records
Show feature table
Start End DB Term Name
798 815 ProSitePatterns PS01156 TonB-dependent receptor proteins signature 2.
798 815 InterPro IPR010917 TonB-dependent receptor, conserved site
1 43 SignalP_GRAM_NEGATIVE SignalP-noTM SignalP-noTM
69 116 Pfam PF07660 Secretin and TonB N terminus short domain
69 116 InterPro IPR011662 Secretin/TonB, short N-terminal domain
44 136 Gene3D G3DSA:3.55.50.30 -
68 118 SMART SM00965 STN_2
68 118 InterPro IPR011662 Secretin/TonB, short N-terminal domain
140 272 FunFam G3DSA:2.170.130.10:FF:000010 Ferripyoverdine receptor
152 815 SUPERFAMILY SSF56935 Porins
139 272 Gene3D G3DSA:2.170.130.10 -
139 272 InterPro IPR037066 TonB-dependent receptor, plug domain superfamily
164 815 NCBIfam TIGR01783 TonB-dependent siderophore receptor
164 815 InterPro IPR010105 TonB-dependent siderophore receptor
1 43 Phobius SIGNAL_PEPTIDE Signal peptide region
1 23 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
162 264 Pfam PF07715 TonB-dependent Receptor Plug Domain
162 264 InterPro IPR012910 TonB-dependent receptor, plug domain
44 815 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
130 815 PANTHER PTHR32552 FERRICHROME IRON RECEPTOR-RELATED
130 815 InterPro IPR039426 TonB-dependent receptor-like
273 815 Gene3D G3DSA:2.40.170.20 -
273 815 InterPro IPR036942 TonB-dependent receptor-like, beta-barrel domain superfamily
36 43 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
168 815 CDD cd01347 ligand_gated_channel
24 35 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
375 813 Pfam PF00593 TonB dependent receptor
375 813 InterPro IPR000531 TonB-dependent receptor-like, beta-barrel

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

11 + 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 5ODW
X-ray 2.80 Å A,B
100.0% 1-815
PDBe RCSB PDBj File
Viewing
PDB 2W16
X-ray 2.71 Å A,B
94.7% 44-815
PDBe RCSB PDBj File
Loaded
PDB 2IAH
X-ray 2.73 Å A
94.7% 44-815
PDBe RCSB PDBj File
Loaded
PDB 2O5P
X-ray 2.77 Å A,B
94.7% 44-815
PDBe RCSB PDBj File
Loaded
PDB 2W76
X-ray 2.80 Å A,B
94.7% 44-815
PDBe RCSB PDBj File
Loaded
PDB 2W6T
X-ray 2.90 Å A,B
94.7% 44-815
PDBe RCSB PDBj File
Loaded
PDB 2W75
X-ray 2.90 Å A,B
94.7% 44-815
PDBe RCSB PDBj File
Loaded
PDB 2W77
X-ray 2.90 Å A,B
94.7% 44-815
PDBe RCSB PDBj File
Loaded
PDB 2W6U
X-ray 3.00 Å A,B
94.7% 44-815
PDBe RCSB PDBj File
Loaded
PDB 2W78
X-ray 3.00 Å A,B
94.7% 44-815
PDBe RCSB PDBj File
Loaded
PDB 1XKH
X-ray 3.60 Å A,B,C
84.3% 129-815
PDBe RCSB PDBj File
Loaded
AlphaFold PA2398
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.

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Ligand Source crystal MW · LogP · TPSA Lipinski PAINS SMILES
N8E
2W16 2.71 Å Open crystal
350.5 Da LogP 2.42 TPSA 66.4 ✓ Ro5 ✓ Clean CCCCCCCCOCCOCCOCCOCCOCCO

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.