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TPR3 of fimv from P. aeruginosa (PAO1)

Analyse TPR3 of fimv from P. aeruginosa (PAO1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4MBQ
Type
protein
Length
301 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Motility protein fimv
UniProt
Q9HZA6
Pockets
2 · best druggability 0.56

Structure

x-ray diffraction · 4 distinct chains · 83% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMotility protein fimvprotein4988% helix, 0% strandQ9HZA6
B, E, FMotility protein fimvprotein5086% helix, 0% strandQ9HZA6
CMotility protein fimvprotein5184% helix, 0% strandQ9HZA6
DMotility protein fimvprotein5175% helix, 0% strandQ9HZA6

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14050.560.7437empty
2500.240.7213empty

Interfaces

9 interfaces between chains.

  • A–E · 412 Ų buried · 9 hydrogen bonds · protein-protein
  • D–F · 379 Ų buried · 4 hydrogen bonds · protein-protein
  • C–D · 378 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 373 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 334 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 4MBQ · TPR3 of FimV from P. aeruginosa (PAO1) · the same entry in another collection · chain F against F, TM-score 1.00
  • Q9HZA6 · AlphaFold monomer V2.0 prediction for motility hub protein fimv (Q9HZA6) · a predicted model of the same protein · chain B against A, TM-score 0.98

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