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MolNFT v1 · #105303 · protein

Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction

4R0X · Peptidyl-prolyl cis-trans isomerase FKBP5: “Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid…”. X-ray diffraction, 1 pocket (best druggability 0.33). MolNFT v1 #105303 on…

PDB
4R0X
Type
protein
Length
122 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-prolyl cis-trans isomerase FKBP5
EC
5.2.1.8
UniProt
Q13451
Pockets
1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8)protein12211% helix, 37% strandQ13451

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.330.7712empty

Compared structures

  • 4R0X · Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q13451 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP5 (Q13451) · a predicted model of the same protein · chain A against A, TM-score 0.97

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