Function and Biology Details
Reaction catalysed:
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107096 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycosyl hydrolase family 13 catalytic domain-containing protein
Molecule details ›
Chains: A, B
Length: 696 amino acids
Theoretical weight: 82.58 KDa
Source organism: Staphylothermus marinus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 696 amino acids
Theoretical weight: 82.58 KDa
Source organism: Staphylothermus marinus
Expression system: Escherichia coli
UniProt:
- Canonical:
A3DM60 (Residues: 1-696; Coverage: 100%)
Sequence domains:
- Maltogenic amylase, N-terminal domain
- Alpha amylase, catalytic domain
- Maltogenic amylase, C-terminal domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
PAL/PLS BEAMLINE 6C1
Spacegroup:
P212121
Expression system: Escherichia coli
