› 6z1h

X-ray diffraction
2.5Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-167914 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
ANCESTRAL RECONSTRUCTED GLYCOSIDASE Chains: A, B
Molecule details ›
Chains: A, B
Length: 459 amino acids
Theoretical weight: 52.61 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
Residues 249 to 266 of chain A and 246 to 258 of chain B could not be identified and has been included as UNK in chain C and D, respectively. Chain: C
Molecule details ›
Chain: C
Length: 18 amino acids
Theoretical weight: 1.55 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
Residues 249 to 266 of chain A and 246 to 258 of chain B could not be identified and has been included as UNK in chain C and D, respectively. Chain: D
Molecule details ›
Chain: D
Length: 13 amino acids
Theoretical weight: 1.12 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

3 bound ligands:
Ligand GOL 2 x GOL
Ligand SO4 1 x SO4
Ligand IPA 1 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P21
Unit cell:
a: 52.263Å b: 80.668Å c: 97.808Å
α: 90° β: 100.061° γ: 90°
R-values:
R R work R free
0.196 0.194 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Ancestral sequence reconstruction - An underused approach to understand the evolution of gene function in plants?
Scossa et al. (2021)
2 more

1 mention without citation

Heme-binding enables allosteric modulation in an ancient TIM-barrel glycosidase.
Gamiz-Arco et al. (2021)