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Structure of cyclophilin a in complex with 4-chloropyrimidin-5-amine

Analyse Structure of cyclophilin a in complex with 4-chloropyrimidin-5-amine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5NOT
Type
protein
Length
165 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-prolyl cis-trans isomerase a
EC
5.2.1.8
UniProt
P62937
Ligands
938

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8)protein16514% helix, 34% strandP62937

Ligands and binding sites

  • 938 · 4-chloranylpyrimidin-5-amine · ligand · 2 copies · chains A

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

Compared structures

  • 5NOT · Structure of cyclophilin A in complex with 4-chloropyrimidin-5-amine · the same entry in another collection · chain A against A, TM-score 1.00

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