› 2x1i

X-ray diffraction
2.36Å resolution

glycoside hydrolase family 77 4-alpha-glucanotransferase from thermus brockianus

Released:
DOI: 10.2210/pdb2x1i/pdb
PDB entry 2x1i coloured by chain, front view.
PDB entry 2x1i coloured by chain, side view.
PDB entry 2x1i coloured by chain, top view.
Source organism: Thermus brockianus
Primary publication:
Structural and functional analysis of substrate recognition by the 250s loop in amylomaltase from Thermus brockianus.
Jung JH, Jung TY, Seo DH, Yoon SM, Choi HC, Park BC, Park CS, Woo EJ
Proteins 79 633-44 (2011)
PMID: 21117235

Function and Biology Details

Reaction catalysed: 
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-alpha-glucanotransferase Chain: A
Molecule details ›
Chain: A
Length: 500 amino acids
Theoretical weight: 57.35 KDa
Source organism: Thermus brockianus
UniProt:
  • Canonical: Q2VJA0 (Residues: 1-500; Coverage: 100%)
Sequence domains: 4-alpha-glucanotransferase
Structure domains: Glycosidases

Ligands and Environments

3 bound ligands:
Ligand PO4 1 x PO4
Ligand SO4 1 x SO4
Ligand INS 2 x INS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P6522
Unit cell:
a: 104.357Å b: 104.357Å c: 263.759Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 0.24

Quick links

Citations

2 review citations

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
1 more

5 mentions without citation

Amylomaltases in Extremophilic Microorganisms.
Leoni et al. (2021)
4 more