› 5cim

X-ray diffraction
3.32Å resolution

Structure of Mycobacterium thermoresistibile GlgE in complex with maltose (cocrystallisation with maltose-1-phosphate) at 3.32A resolution

Released:
DOI: 10.2210/pdb5cim/pdb
Model geometry
Fit model/data
PDB entry 5cim coloured by chain, front view.
PDB entry 5cim coloured by chain, side view.
PDB entry 5cim coloured by chain, top view.
Source organism: Mycolicibacterium thermoresistibile ATCC 19527
Primary publication:
Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism.
Mendes V, Blaszczyk M, Maranha A, Empadinhas N, Blundell TL
OpenAccess logo Sci Rep 5 17144 (2015)
PMID: 26616850

Function and Biology Details

Reaction catalysed: 
Alpha-maltose 1-phosphate + ((1->4)-alpha-D-glucosyl)(n) = phosphate + ((1->4)-alpha-D-glucosyl)(n+2)
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-124558 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 698 amino acids
Theoretical weight: 77.62 KDa
Source organism: Mycolicibacterium thermoresistibile ATCC 19527
Expression system: Escherichia coli
UniProt:
  • Canonical: G7CL00 (Residues: 2-696; Coverage: 100%)
Gene names: KEK_12948, glgE
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 77.537Å b: 112.967Å c: 221.433Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.214
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Ligand-bound Structures and Site-directed Mutagenesis Identify the Acceptor and Secondary Binding Sites of Streptomyces coelicolor Maltosyltransferase GlgE.
Syson et al. (2016)

3 mentions without citation

Sensitive quantification of carbon monoxide in vivo reveals a protective role of circulating hemoglobin in CO intoxication.
Mao et al. (2021)
2 more