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Structure of Cyclophilin D Peptidyl-Prolyl Isomerase Domain bound to Macrocyclic Inhibitor B21

Analyse Structure of Cyclophilin D Peptidyl-Prolyl Isomerase Domain bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7TH6
Type
protein
Length
163 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
0.97
Source
Homo sapiens
Molecule
Peptidyl-prolyl cis-trans isomerase F, mitochondrial
EC
5.2.1.8
UniProt
P30405
Ligands
I56

Structure

x-ray diffraction · resolution 0.97 · 1 distinct chain · 15% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase F, mitochondrial (EC 5.2.1.8)protein16315% helix, 34% strandP30405

Ligands and binding sites

  • I56 · 4'-{[(4S,7S,11R,13E,19S)-19-{[2-(2-aminoethoxy)ethyl]carbamoyl}-7-benzyl-3,6,12,15,21-pentaoxo-1,3,4,5,6,7,8,9,10,12,15,16,17,18,19,20,21,22-octadecahydro-2H-7,11-methano-2,5,11,16,20-benzopentaazacyclotetracosin-4-yl]methyl}-2-methyl[1,1'-biphenyl]-4-carboxylic acid · ligand · chains A

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

Compared structures

  • 7TH6 · Structure of cyclophilin D peptidyl-prolyl isomerase domain bound to macrocyclic… · the same entry in another collection · chain A against A, TM-score 1.00
  • P30405 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase F… · a predicted model of the same protein · chain A against A, TM-score 0.99

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