› 5gm4

X-ray diffraction
1.92Å resolution

Crystal structure of FI-CMCase from Aspergillus aculeatus F-50 in complex with cellotetrose

Released:
DOI: 10.2210/pdb5gm4/pdb
PDB entry 5gm4 coloured by chain, front view.
PDB entry 5gm4 coloured by chain, side view.
PDB entry 5gm4 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-540262 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endoglucanase-1 Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 219 amino acids
Theoretical weight: 23.72 KDa
Source organism: Aspergillus aculeatus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P22669 (Residues: 19-237; Coverage: 99%)
Sequence domains: Glycosyl hydrolase family 12
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
1 bound ligand:
Ligand SO4 8 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P21
Unit cell:
a: 87.907Å b: 85.278Å c: 106.025Å
α: 90° β: 92.47° γ: 90°
R-values:
R R work R free
0.158 0.156 0.207
Expression system: Komagataella pastoris

Quick links

Citations

3 citation in other articles

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

1 mention without citation

Characterization of the Biomass Degrading Enzyme GuxA from Acidothermus cellulolyticus.
Hengge et al. (2022)