› 6uas

X-ray diffraction
1.91Å resolution

Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199A mutant) from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaripentaose

Released:
DOI: 10.2210/pdb6uas/pdb
PDB entry 6uas coloured by chain, front view.
PDB entry 6uas coloured by chain, side view.
PDB entry 6uas coloured by chain, top view.
Source organism: Amycolatopsis mediterranei
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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-220566 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glycoside Hydrolase Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 27.86 KDa
Source organism: Amycolatopsis mediterranei
Expression system: Escherichia coli

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer
3 bound ligands:
Ligand BGC 1 x BGC
Ligand ZN 1 x ZN
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P21
Unit cell:
a: 36.68Å b: 79.347Å c: 46.152Å
α: 90° β: 103.11° γ: 90°
R-values:
R R work R free
0.159 0.157 0.198
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Discovery of new enzymatic functions and metabolic pathways using genomic enzymology web tools.
Zallot et al. (2021)
4 more