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The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((3,5- DICHLOROPHENYL)SULFONYL)-5-(hydroxymethyl)-3-(pyridin-2-ylmethyl)-3, 10-DIAZABICYCLO[4.3.1]DECAN-2-one

Analyse The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((3,5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5OBK
Type
protein
Length
128 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
Ligands
9QN
Pockets
1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8)protein12817% helix, 35% strandQ13451

Ligands and binding sites

  • 9QN · (1~{S},5~{S},6~{R})-10-[3,5-bis(chloranyl)phenyl]sulfonyl-5-(hydroxymethyl)-3-(pyridin-2-ylmethyl)-3,10-diazabicyclo[4.3.1]decan-2-one · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1910.430.78149QN

Compared structures

  • 5OBK · The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-((3,5-dichlorophenyl)sulfonyl)-5-(h… · 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 0.99

Analyse

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