› 1fp8

X-ray diffraction
2.3Å resolution

STRUCTURE OF THE AMYLOMALTASE FROM THERMUS THERMOPHILUS HB8 IN SPACE GROUP P21212

Released:
DOI: 10.2210/pdb1fp8/pdb
PDB 1fp8 coloured by chain and viewed from the front.
PDB 1fp8 coloured by chain and viewed from the side.
PDB 1fp8 coloured by chain and viewed from the top.
Source organism: Thermus thermophilus
Entry authors: Uitdehaag JCM, Euverink GJ, van der Veen BA, van der Maarel M, Dijkstra BW

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-alpha-glucanotransferase Chain: A
Molecule details ›
Chain: A
Length: 500 amino acids
Theoretical weight: 57.26 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: O87172 (Residues: 1-500; Coverage: 100%)
Gene name: malQ
Sequence domains: 4-alpha-glucanotransferase
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
Ligand HG 1 x HG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21212
Unit cell:
a: 115.234Å b: 93.67Å c: 53.463Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.232
Expression system: Escherichia coli

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