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Crystal structure of mouse peptide N-glycanase C-terminal domain in complex with mannopentaose

Analyse Crystal structure of mouse peptide N-glycanase C-terminal domain in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2I74
Type
protein
Length
360 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pngase
EC
3.5.1.52
UniProt
Q9JI78
Ligands
MAN
Pockets
1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPngase (EC 3.5.1.52)protein18011% helix, 51% strandQ9JI78

Ligands and binding sites

  • MAN · alpha-D-mannopyranose · sugar · 8 copies · chains A, B
  • ACT · Acetate ion · additive · 6 copies · chains A, B
  • GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12280.560.7926empty

Interfaces

1 interface between chains.

  • A–B · 863 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 2I74 · Crystal structure of mouse Peptide N-Glycanase C-terminal domain in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9JI78 · AlphaFold monomer V2.0 prediction for peptide-N(4)-(N-acetyl-beta… · a predicted model of the same protein · chain A against A, TM-score 0.99

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