› 5gm3

X-ray diffraction
1.59Å resolution

Crystal structure of FI-CMCase from Aspergillus aculeatus F-50

Released:
DOI: 10.2210/pdb5gm3/pdb
PDB entry 5gm3 coloured by chain, front view.
PDB entry 5gm3 coloured by chain, side view.
PDB entry 5gm3 coloured by chain, top view.
Source organism: Aspergillus aculeatus
Primary publication:
Crystal structure and genetic modifications of FI-CMCase from Aspergillus aculeatus F-50.
Huang JW, Liu W, Lai HL, Cheng YS, Zheng Y, Li Q, Sun H, Kuo CJ, Guo RT, Chen CC
Biochem Biophys Res Commun 478 565-72 (2016)
PMID: 27470581

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoglucanase-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 23.78 KDa
Source organism: Aspergillus aculeatus
Expression system: Escherichia coli
UniProt:
  • Canonical: P22669 (Residues: 19-237; Coverage: 99%)
Sequence domains: Glycosyl hydrolase family 12
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand ZN 8 x ZN
Ligand CAC 4 x CAC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: C2221
Unit cell:
a: 74.215Å b: 75.089Å c: 188.385Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.157 0.19
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Plant receptor-like protein activation by a microbial glycoside hydrolase.
Sun et al. (2022)
3 more

1 mention without citation

Salt-tolerant and thermostable mechanisms of an endoglucanase from marine Aspergillus niger.
Cai et al. (2022)