› 6p2m

X-ray diffraction
1.98Å resolution

Crystal structure of the Caldicellulosiruptor lactoaceticus GH74 (ClGH74a) enzyme in complex with LLG xyloglucan

Released:
DOI: 10.2210/pdb6p2m/pdb
PDB entry 6p2m coloured by chain, front view.
PDB entry 6p2m coloured by chain, side view.
PDB entry 6p2m coloured by chain, top view.
Source organism: Caldicellulosiruptor lactoaceticus 6A
Primary publication:
Substrate specificity, regiospecificity, and processivity in glycoside hydrolase family 74.
Arnal G, Stogios PJ, Asohan J, Attia MA, Skarina T, Viborg AH, Henrissat B, Savchenko A, Brumer H
J Biol Chem 294 13233-13247 (2019)
PMID: 31324716

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124271 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
CBM3 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 696 amino acids
Theoretical weight: 74.67 KDa
Source organism: Caldicellulosiruptor lactoaceticus 6A
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: G2PXX7 (Residues: 35-726; Coverage: 53%)
Gene name: Calla_2311

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, XYS, GAL
Carbohydrate polymer
3 bound ligands:
Ligand PE3 1 x PE3
Ligand GOL 4 x GOL
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 64.994Å b: 72.759Å c: 150.703Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.156 0.204
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Cell Surface Xyloglucan Recognition and Hydrolysis by the Human Gut Commensal Bacteroides uniformis.
Grondin et al. (2022)
1 more

2 mentions without citation

Substrate specificity, regiospecificity, and processivity in glycoside hydrolase family 74.
Arnal et al. (2019)
1 more