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Crystal structure of the rrm domain of cyclophilin 33

Analyse Crystal structure of the rrm domain of cyclophilin 33 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3MDF
Type
protein
Length
166 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-prolyl cis-trans isomerase E
EC
5.2.1.8
UniProt
Q9UNP9
Pockets
2 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPeptidyl-prolyl cis-trans isomerase E (EC 5.2.1.8)protein8327% helix, 34% strandQ9UNP9

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.320.7713empty
2590.300.7515empty

Interfaces

1 interface between chains.

  • A–B · 611 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 3MDF · Crystal structure of the RRM domain of Cyclophilin 33 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UNP9 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase E (Q9UNP9) · a predicted model of the same protein · chain A against A, TM-score 0.94

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