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Crystal structure of human FKBP51 FK1 domain A19T mutant in complex with imidazole

Analyse Crystal structure of human FKBP51 FK1 domain A19T mutant in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6TX8
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
NA, CL
Pockets
1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8)protein12817% helix, 36% strandQ13451

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains A
  • CL · Chloride ion · ion · chains A
  • IMD · Imidazole · additive · 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
1660.390.7916IMD

Compared structures

  • 6TX8 · Crystal structure of human FKBP51 FK1 domain A19T mutant in complex with imidazole · 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 0.98

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