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Crystal structure of human glutaminyl cyclase at pH 6.5

Analyse Crystal structure of human glutaminyl cyclase at pH 6.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2AFM
Type
protein
Length
646 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutaminyl-peptide cyclotransferase
EC
2.3.2.5
UniProt
Q16769
Ligands
ZN, SO4
Pockets
5 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGlutaminyl-peptide cyclotransferase (EC 2.3.2.5)protein32338% helix, 16% strandQ16769

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15870.670.7779empty
2910.490.8219SO4
3520.380.8017SO4
4690.330.7618empty
5580.300.7617empty

Interfaces

1 interface between chains.

  • A–B · 553 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 2AFM · Crystal structure of human glutaminyl cyclase at pH 6.5 · the same entry in another collection · chain A against A, 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 1.00

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