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Structural analysis of protein folding by the methanococcus jannaschii chaperone FKBP26

Analyse Structural analysis of protein folding by the methanococcus jannaschii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3PRB
Type
protein
Length
447 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fkbp-type peptidyl-prolyl cis-trans isomerase
EC
5.2.1.8
UniProt
Q58235
Pockets
3 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFkbp-type peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)protein22324% helix, 35% strandQ58235
BFkbp-type peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)protein22425% helix, 33% strandQ58235

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11670.450.7525empty
21230.410.7520empty
31000.340.7321empty

Interfaces

1 interface between chains.

  • A–B · 991 Ų buried · 27 hydrogen bonds · protein-protein

Compared structures

  • 3PRB · Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q58235 · AlphaFold monomer V2.0 prediction for long-type peptidyl-prolyl cis- trans isomerase… · a predicted model of the same protein · chain A against A, TM-score 0.89

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