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Atomic resolution crystal structure of the ppiase domain of human cyclophilin G in complex with cyclosporin a.

Analyse Atomic resolution crystal structure of the ppiase domain of human cyclophilin G… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WFJ
Type
protein
Length
183 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-prolyl cis-trans isomerase G; Cyclosporin a
EC
5.2.1.8
UniProt
Q13427
Ligands
MG, CL

Structure

x-ray diffraction · 2 distinct chains · 13% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase G (EC 5.2.1.8)protein17213% helix, 33% strandQ13427
BCyclosporin aprotein110% helix, 9% strand—

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A
  • CL · Chloride ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · chains A

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

Interfaces

1 interface between chains.

  • A–B · 484 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified, 1 d-amino (nonstandard, methylation, D-amino acid).

Compared structures

  • 2WFJ · Atomic resolution crystal structure of the PPIase domain of human cyclophilin G in… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q13427 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase G (Q13427) · a predicted model of the same protein · chain A against A, TM-score 0.99

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