› 4ac1

X-ray diffraction
1.3Å resolution

The structure of a fungal endo-beta-N-acetylglucosaminidase from glycosyl hydrolase family 18, at 1.3A resolution

Released:
DOI: 10.2210/pdb4ac1/pdb
Model geometry
Fit model/data
PDB entry 4ac1 coloured by chain, front view.
PDB entry 4ac1 coloured by chain, side view.
PDB entry 4ac1 coloured by chain, top view.
Source organism: Trichoderma reesei
Primary publication:
High resolution crystal structure of the endo-N-Acetyl-β-D-glucosaminidase responsible for the deglycosylation of Hypocrea jecorina cellulases.
Stals I, Karkehabadi S, Kim S, Ward M, Van Landschoot A, Devreese B, Sandgren M
OpenAccess logo PLoS One 7 e40854 (2012)
PMID: 22859955

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)(2))Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein, the rest of the oligosaccharide is released intact.
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111406 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GH18 domain-containing protein Chain: X
Molecule details ›
Chain: X
Length: 283 amino acids
Theoretical weight: 30.94 KDa
Source organism: Trichoderma reesei
UniProt:
  • Canonical: C4RA89 (Residues: 31-313; Coverage: 83%)
Gene name: endoT
Structure domains: Glycosidases

Ligands and Environments

3 bound ligands:
Ligand NAG 2 x NAG
Ligand ACT 3 x ACT
Ligand ZN 8 x ZN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P21
Unit cell:
a: 35.438Å b: 63.874Å c: 59.36Å
α: 90° β: 100.97° γ: 90°
R-values:
R R work R free
0.185 0.184 0.202

Quick links

Citations

2 review citations

The ENGases: versatile biocatalysts for the production of homogeneous N-linked glycopeptides and glycoproteins.
Fairbanks AJ. (2017)
1 more

7 mentions without citation

Sculpting therapeutic monoclonal antibody N-glycans using endoglycosidases.
Trastoy et al. (2022)
6 more