› 3n98

X-ray diffraction
1.87Å resolution

Crystal structure of TK1436, a GH57 branching enzyme from hyperthermophilic archaeon Thermococcus kodakaraensis, in complex with glucose and additives

Released:
DOI: 10.2210/pdb3n98/pdb
PDB entry 3n98 coloured by chain, front view.
PDB entry 3n98 coloured by chain, side view.
PDB entry 3n98 coloured by chain, top view.
Source organism: Thermococcus kodakarensis
Primary publication:
Structural basis for branching-enzyme activity of glycoside hydrolase family 57: structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.
Santos CR, Tonoli CC, Trindade DM, Betzel C, Takata H, Kuriki T, Kanai T, Imanaka T, Arni RK, Murakami MT
Proteins 79 547-57 (2011)
PMID: 21104698

Function and Biology Details

Reaction catalysed: 
Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1,4-alpha-glucan branching enzyme TK1436 Chain: A
Molecule details ›
Chain: A
Length: 562 amino acids
Theoretical weight: 66.17 KDa
Source organism: Thermococcus kodakarensis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5JDJ7 (Residues: 1-562; Coverage: 83%)
Gene name: TK1436
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand BGC 3 x BGC
Ligand GOL 3 x GOL
Ligand DIO 2 x DIO
Ligand PEG 1 x PEG
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 70.674Å b: 79.02Å c: 134.088Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.159 0.196
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

1 mention without citation

Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity.
Zhang et al. (2019)