› 2z1k

X-ray diffraction
2.3Å resolution

Crystal Structure of Ttha1563 from Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb2z1k/pdb
PDB entry 2z1k coloured by chain, front view.
PDB entry 2z1k coloured by chain, side view.
PDB entry 2z1k coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Entry authors: Niwa H, Shimada A, Matsunaga E, Kuramitsu S, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-177926 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Glycosyl hydrolase family 13 catalytic domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 475 amino acids
Theoretical weight: 54.2 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SI17 (Residues: 1-475; Coverage: 100%)
Gene name: TTHA1563
Sequence domains: Alpha amylase, catalytic domain
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand PO4 1 x PO4
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P21
Unit cell:
a: 67.144Å b: 95.897Å c: 140.598Å
α: 90° β: 94.4° γ: 90°
R-values:
R R work R free
0.185 0.185 0.236
Expression system: Escherichia coli

Quick links