Crystal structure of human glutaminyl cyclase in complex with GLU(GAMMA-hydrazide)-phe-ala

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 16% strand (DSSP).

Ligands and binding sites

• ORT · (4~{S})-4-azanyl-5-oxidanylidene-pentanehydrazide · ligand · 3 copies · chains A, B
• PHE · Phenylalanine · ligand · 3 copies · chains A, B
• 66N · L-alaninamide · ligand · 3 copies · chains A, B
• ZN · Zinc ion · metal · 10 copies · chains A, B
• SO4 · Sulfate ion · ion · 11 copies · chains A, B
• GOL · Glycerol · additive · 5 copies · chains A, B
• PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A, B
• PG4 · Tetraethylene glycol · additive · 3 copies · chains A
• PGE · Triethylene glycol · additive · 2 copies · chains B
• MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains B
• DIO · 1,4-diethylene dioxide · additive · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 531 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

• 6YI1 · Crystal structure of human glutaminyl cyclase in complex with Glu(gamma-hydrazide)-Phe-Ala · the same entry in another collection · chain B against B, TM-score 1.00
• Q16769 · AlphaFold monomer V2.0 prediction for glutaminyl-peptide cyclotransferase (Q16769) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q16769
• Elsewhere: RCSB PDB 6YI1 · PDBe 6YI1 · UniProt Q16769