› 6uaz

X-ray diffraction
1.85Å resolution

Crystal structure of a GH128 (subgroup III) curdlan-specific exo-beta-1,3-glucanase from Blastomyces gilchristii (BgGH128_III) in complex with glucose

Released:
DOI: 10.2210/pdb6uaz/pdb
PDB entry 6uaz coloured by chain, front view.
PDB entry 6uaz coloured by chain, side view.
PDB entry 6uaz coloured by chain, top view.
Source organism: Blastomyces gilchristii
Primary publication:
Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family.
Santos CR, Costa PACR, Vieira PS, Gonzalez SET, Correa TLR, Lima EA, Mandelli F, Pirolla RAS, Domingues MN, Cabral L, Martins MP, Cordeiro RL, Junior AT, Souza BP, Prates ÉT, Gozzo FC, Persinoti GF, Skaf MS, Murakami MT
Nat Chem Biol 16 920-929 (2020)
PMID: 32451508

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103148 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Asl1-like glycosyl hydrolase catalytic domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 261 amino acids
Theoretical weight: 27.99 KDa
Source organism: Blastomyces gilchristii
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A179UGT5 (Residues: 23-262; Coverage: 100%)
Gene name: BDBG_03339
Sequence domains: Glycosyl hydrolase catalytic core

Ligands and Environments

1 bound ligand:
Ligand BGC 2 x BGC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P1
Unit cell:
a: 36.46Å b: 48.928Å c: 57.757Å
α: 102.97° β: 89.34° γ: 93.76°
R-values:
R R work R free
0.167 0.164 0.217
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Recent advances in enzymatic synthesis of β-glucan and cellulose.
Bulmer et al. (2021)
4 more