› 3voc

X-ray diffraction
1.95Å resolution

Crystal structure of the catalytic domain of beta-amylase from paenibacillus polymyxa

Released:
DOI: 10.2210/pdb3voc/pdb
PDB entry 3voc coloured by chain, front view.
PDB entry 3voc coloured by chain, side view.
PDB entry 3voc coloured by chain, top view.
Source organism: Paenibacillus polymyxa
Entry authors: Nishimura S, Fujioka T, Nakaniwa T, Tada T

Function and Biology Details

Reactions catalysed: 
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta/alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 419 amino acids
Theoretical weight: 45.85 KDa
Source organism: Paenibacillus polymyxa
Expression system: Escherichia coli
UniProt:
  • Canonical: P21543 (Residues: 36-454; Coverage: 36%)
Sequence domains: Glycosyl hydrolase family 14
Structure domains: Glycosidases

Ligands and Environments

6 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
Ligand EDO 3 x EDO
Ligand GOL 3 x GOL
Ligand TRS 2 x TRS
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 61.028Å b: 68.519Å c: 93.904Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.19
Expression system: Escherichia coli

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