› 5n0f

X-ray diffraction
1.69Å resolution

The catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with 1,6-ManSIFG

Released:
DOI: 10.2210/pdb5n0f/pdb
PDB 5n0f coloured by chain and viewed from the front.
PDB 5n0f coloured by chain and viewed from the side.
PDB 5n0f coloured by chain and viewed from the top.
Source organism: Niallia circulans
Primary publication:
An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-��-mannanase inhibitor.
Belz T, Jin Y, Coines J, Rovira C, Davies GJ, Williams SJ
Chem. Commun. (Camb.) (2017)
PMID: 28766587

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CBM6 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 362 amino acids
Theoretical weight: 40.93 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Z4P9 (Residues: 35-375; Coverage: 61%)
Gene name: aman6
Sequence domains: Glycosyl hydrolase family 76
Structure domains: Glycosyltransferase

Ligands and Environments

1 bound ligand:
Ligand 7K2 2 x 7K2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 85.05Å b: 86.4Å c: 103.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.152 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Development of Non-Hydrolysable Oligosaccharide Activity-Based Inactivators for Endoglycanases: A Case Study on α-1,6 Mannanases.
Schröder et al. (2021)
2 more