› 1olq

X-ray diffraction
1.7Å resolution

The Trichoderma reesei cel12a P201C mutant, structure at 1.7 A resolution

Released:
DOI: 10.2210/pdb1olq/pdb
PDB entry 1olq coloured by chain, front view.
PDB entry 1olq coloured by chain, side view.
PDB entry 1olq coloured by chain, top view.
Source organism: Trichoderma reesei
Primary publication:
The Humicola grisea Cel12A enzyme structure at 1.2 A resolution and the impact of its free cysteine residues on thermal stability.
Sandgren M, Gualfetti PJ, Paech C, Paech S, Shaw A, Gross LS, Saldajeno M, Berglund GI, Jones TA, Mitchinson C
Protein Sci 12 2782-93 (2003)
PMID: 14627738

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126115 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-beta-1,4-glucanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 218 amino acids
Theoretical weight: 23.48 KDa
Source organism: Trichoderma reesei
Expression system: Aspergillus niger
UniProt:
  • Canonical: O00095 (Residues: 17-234; Coverage: 100%)
Gene name: egl
Sequence domains: Glycosyl hydrolase family 12
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand NAG 2 x NAG
1 modified residue:
Ligand PCA 2 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P31
Unit cell:
a: 70.616Å b: 70.616Å c: 69.092Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.209 0.251
Expression system: Aspergillus niger

Quick links

Citations

18 citation in other articles

Consistent mutational paths predict eukaryotic thermostability.
van Noort et al. (2013)
17 more

3 mentions without citation

The Humicola grisea Cel12A enzyme structure at 1.2 A resolution and the impact of its free cysteine residues on thermal stability.
Sandgren et al. (2003)
2 more