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› 6a0k

X-ray diffraction
1.94Å resolution

Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from Arthrobacter globiformis, complex with panose

Released:
DOI: 10.2210/pdb6a0k/pdb
Model geometry
Fit model/data
PDB entry 6a0k coloured by chain, front view.
PDB entry 6a0k coloured by chain, side view.
PDB entry 6a0k coloured by chain, top view.
Source organism: Arthrobacter globiformis
Primary publication:
Structural features of a bacterial cyclic α-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis.
Kohno M, Arakawa T, Ota H, Mori T, Nishimoto T, Fushinobu S
J Biol Chem 293 16874-16888 (2018)
PMID: 30181215

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Glycosyl hydrolase family 13 catalytic domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 471 amino acids
Theoretical weight: 51.66 KDa
Source organism: Arthrobacter globiformis
Expression system: Escherichia coli
UniProt:
  • Canonical: D2YYE1 (Residues: 2-450; Coverage: 100%)
Gene name: cmmF
Sequence domains: Alpha amylase, catalytic domain

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC, BGC
Carbohydrate polymer
1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21
Unit cell:
a: 48.293Å b: 180.225Å c: 62.926Å
α: 90° β: 111.6° γ: 90°
R-values:
R R work R free
0.189 0.188 0.223
Expression system: Escherichia coli

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Citations

2 citation in other articles

A Novel Subfamily GH13_46 of the α-Amylase Family GH13 Represented by the Cyclomaltodextrinase from Flavobacterium sp. No. 92.
Mareček et al. (2022)
1 more

1 mention without citation

Structural features of a bacterial cyclic α-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis.
Kohno et al. (2018)