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Cyclophilin a complexed with tri-vector ligand 10.

Analyse Cyclophilin a complexed with tri-vector ligand 10. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GJL
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
F1Q
Pockets
1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8)protein16514% helix, 33% strandP62937

Ligands and binding sites

  • F1Q · ethyl 2-[[(4-aminophenyl)methyl-(1~{H}-1,2,3,4-tetrazol-5-ylmethyl)carbamoyl]amino]ethanoate · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1630.330.7716F1Q

Compared structures

  • 6GJL · Cyclophilin A complexed with tri-vector ligand 10. · the same entry in another collection · chain A against A, TM-score 1.00

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