› 7nl5

X-ray diffraction
1.4Å resolution

Structure of the catalytic domain of the Bacillus circulans alpha-1,6 Mannanase in complex with an alpha-1,6-alpha-manno-cyclophellitol trisaccharide inhibitor

Released:
DOI: 10.2210/pdb7nl5/pdb
PDB entry 7nl5 coloured by chain, front view.
PDB entry 7nl5 coloured by chain, side view.
PDB entry 7nl5 coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Development of Non-Hydrolysable Oligosaccharide Activity-Based Inactivators for Endoglycanases: A Case Study on α-1,6 Mannanases.
Schröder SP, Offen WA, Males A, Jin Y, de Boer C, Enotarpi J, Marino L, van der Marel GA, Florea BI, Codée JDC, Overkleeft HS, Davies GJ
OpenAccess logo Chemistry 27 9519-9523 (2021)
PMID: 33878235

Function and Biology Details

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-195578 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
CBM6 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 362 amino acids
Theoretical weight: 40.93 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Z4P9 (Residues: 35-375; Coverage: 58%)
Gene name: aman6
Sequence domains: Glycosyl hydrolase family 76

Ligands and Environments

Carbohydrate polymer : NEW Components: MAN
Carbohydrate polymer
2 bound ligands:
Ligand UKQ 1 x UKQ
Ligand UKT 1 x UKT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 43.521Å b: 65.415Å c: 49.442Å
α: 90° β: 101.9° γ: 90°
R-values:
R R work R free
0.148 0.147 0.173
Expression system: Escherichia coli

Quick links

Citations

1 citations 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)