› 6p2o

X-ray diffraction
1.88Å resolution

Crystal structure of Streptomyces rapamycinicus GH74 in complex with xyloglucan fragments XLLG and XXXG

Released:
DOI: 10.2210/pdb6p2o/pdb
PDB entry 6p2o coloured by chain, front view.
PDB entry 6p2o coloured by chain, side view.
PDB entry 6p2o coloured by chain, top view.
Source organism: Streptomyces rapamycinicus NRRL 5491
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:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100778 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Xyloglucanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 727 amino acids
Theoretical weight: 77.52 KDa
Source organism: Streptomyces rapamycinicus NRRL 5491
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0A0NH71 (Residues: 46-772; Coverage: 98%)
Gene name: D3C57_132765

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, XYS, GAL
Carbohydrate polymer
Carbohydrate polymer : NEW Components: BGC, XYS
Carbohydrate polymer
3 bound ligands:
Ligand SO4 8 x SO4
Ligand GOL 7 x GOL
Ligand CL 7 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 92.996Å b: 112.788Å c: 222.759Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.148 0.18
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

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

1 mention without citation

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