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Crystal structure of cyclophilin from trypanosoma cruzi

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

PDB
1XO7
Type
protein
Length
664 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cyclophilin
UniProt
Q4DPB9
Pockets
5 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DCyclophilinprotein16616% helix, 35% strandQ4DPB9

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12510.620.8144empty
2940.420.7826empty
31130.370.7422empty
4790.370.7723empty
5750.350.7620empty

Interfaces

2 interfaces between chains.

  • B–C · 659 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 319 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 1XO7 · Crystal structure of cyclophilin from Trypanosoma cruzi · the same entry in another collection · chain A against A, TM-score 1.00

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