› 1tvp

X-ray diffraction
1.6Å resolution

Endoglucanase cel5G from Pseudoalteromonas haloplanktis in complex with cellobiose

Released:
DOI: 10.2210/pdb1tvp/pdb
PDB entry 1tvp coloured by chain, front view.
PDB entry 1tvp coloured by chain, side view.
PDB entry 1tvp coloured by chain, top view.
Source organism: Pseudoalteromonas haloplanktis
Primary publication:
Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering.
Violot S, Aghajari N, Czjzek M, Feller G, Sonan GK, Gouet P, Gerday C, Haser R, Receveur-Bréchot V
J Mol Biol 348 1211-24 (2005)
PMID: 15854656

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131457 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Chitin-binding type-3 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 293 amino acids
Theoretical weight: 31.91 KDa
Source organism: Pseudoalteromonas haloplanktis
Expression system: Escherichia coli
UniProt:
  • Canonical: O86099 (Residues: 33-325; Coverage: 63%)
Gene name: celG
Sequence domains: Cellulase (glycosyl hydrolase family 5)
Structure domains: Glycosidases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 135.5Å b: 78.9Å c: 44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.158 0.189
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Cold-adapted enzymes.
Siddiqui et al. (2006)
13 more

4 mentions without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
3 more