Protein profile

PA1083

flagellar basal body L-ring protein

Genome: NC_002516.2

Gene: PA1083 flgH Structure source: AlphaFold UniProt Q9I4P6
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Amino acids 231
Annotations 4
Features 25
PDB binders 1
Druggability 0.659

Overview

Basic information about this protein and its source genome.

Accession
PA1083
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1083 flgH
Status
annotated
Amino acids
231
Structure source
AlphaFold
GO
GO:0009427 One of the rings of the bacterial-type flagellar basal body; anchors the basal body to the outer membrane. 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:0003774 Generation of force resulting in movement, for example along a microfilament or microtubule, or in torque resulting in membrane scission or rotation of a flagellum. The energy required is obtained either from the hydrolysis of a nucleoside triphosphate or by an electrochemical proton gradient (proton-motive force). GO:0071973 Cell motility due to the motion of one or more bacterial-type flagella. A bacterial-type flagellum is a motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope.

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 0.659
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:0009427 One of the rings of the bacterial-type flagellar basal body; anchors the basal body to the outer membrane.
  • 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:0003774 Generation of force resulting in movement, for example along a microfilament or microtubule, or in torque resulting in membrane scission or rotation of a flagellum. The energy required is obtained either from the hydrolysis of a nucleoside triphosphate or by an electrochemical proton gradient (proton-motive force).
  • GO:0071973 Cell motility due to the motion of one or more bacterial-type flagella. A bacterial-type flagellum is a motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records
Show feature table
Start End DB Term Name
4 12 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
118 138 MobiDBLite mobidb-lite consensus disorder prediction
1 17 SignalP_EUK SignalP-noTM SignalP-noTM
1 17 Phobius SIGNAL_PEPTIDE Signal peptide region
1 15 SignalP_GRAM_POSITIVE SignalP-TM SignalP-TM
13 17 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
1 3 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
207 221 PRINTS PR01008 Flagellar L-ring protein signature
207 221 InterPro IPR000527 Flagellar L-ring protein
170 186 PRINTS PR01008 Flagellar L-ring protein signature
170 186 InterPro IPR000527 Flagellar L-ring protein
66 78 PRINTS PR01008 Flagellar L-ring protein signature
66 78 InterPro IPR000527 Flagellar L-ring protein
191 205 PRINTS PR01008 Flagellar L-ring protein signature
191 205 InterPro IPR000527 Flagellar L-ring protein
144 159 PRINTS PR01008 Flagellar L-ring protein signature
144 159 InterPro IPR000527 Flagellar L-ring protein
1 19 ProSiteProfiles PS51257 Prokaryotic membrane lipoprotein lipid attachment site profile.
1 228 Hamap MF_00415 Flagellar L-ring protein [flgH].
1 228 InterPro IPR000527 Flagellar L-ring protein
1 231 PANTHER PTHR34933 FLAGELLAR L-RING PROTEIN
1 231 InterPro IPR000527 Flagellar L-ring protein
44 230 Pfam PF02107 Flagellar L-ring protein
44 230 InterPro IPR000527 Flagellar L-ring protein
18 231 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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

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 PA1083
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
2 0.659
9 0.556
5 0.207

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.

51 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
OCA
7CBL
P0A1N8 144.2 Da LogP 2.43 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCC(=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.