› 2zum

X-ray diffraction
1.95Å resolution

Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb2zum/pdb
PDB entry 2zum coloured by chain, front view.
PDB entry 2zum coloured by chain, side view.
PDB entry 2zum coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Structure of hyperthermophilic endocellulase from Pyrococcus horikoshii.
Kim HW, Ishikawa K
Proteins 78 496-500 (2010)
PMID: 19847920

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycoside hydrolase family 5 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 458 amino acids
Theoretical weight: 51.95 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O58925 (Residues: 1-458; Coverage: 100%)
Gene name: PH1171
Sequence domains: Cellulase (glycosyl hydrolase family 5)
Structure domains: Glycosidases

Ligands and Environments

3 bound ligands:
Ligand ACT 2 x ACT
Ligand ZN 8 x ZN
Ligand GOL 8 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P41212
Unit cell:
a: 77.15Å b: 77.15Å c: 161.105Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Biomass-degrading glycoside hydrolases of archaeal origin.
Suleiman et al. (2020)
1 more

5 mentions without citation

Tracing determinants of dual substrate specificity in glycoside hydrolase family 5.
Chen et al. (2012)
4 more