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MolNFT v1 · #56418 · protein

Crystal structure of the human glutaminyl cyclase mutant D305A at 1.78 ångström resolution

2ZEN · Glutaminyl-peptide cyclotransferase: “Crystal structure of the human glutaminyl cyclase mutant D305A at 1.78 ångström resolution”. X-ray diffraction, 2 ligands (ZN, SO4), 2 pockets (best druggability 0.70). MolNFT v1 #56418 on…

PDB
2ZEN
Type
protein
Length
644 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
2 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutaminyl-peptide cyclotransferase (EC 2.3.2.5)protein32337% helix, 16% strandQ16769
BGlutaminyl-peptide cyclotransferase (EC 2.3.2.5)protein32140% helix, 19% 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

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17480.700.77104empty
2900.510.8319SO4

Interfaces

1 interface between chains.

  • A–B · 566 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 2ZEN · Crystal structure of the human glutaminyl cyclase mutant D305A at 1.78 angstrom resolution · 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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