PDBe 1cb7

X-ray diffraction
2Å resolution

GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM RECONSTITUTED WITH METHYL-COBALAMIN

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutamate mutase sigma subunit Chains: A, C
Molecule details ›
Chains: A, C
Length: 137 amino acids
Theoretical weight: 14.83 KDa
Source organism: Clostridium cochlearium
Expression system: Escherichia coli
UniProt:
  • Canonical: P80078 (Residues: 1-137; Coverage: 100%)
Gene name: glmS
Sequence domains: B12 binding domain
Structure domains: Cobalamin (vitamin B12)-binding domain
Glutamate mutase epsilon subunit Chains: B, D
Molecule details ›
Chains: B, D
Length: 483 amino acids
Theoretical weight: 53.62 KDa
Source organism: Clostridium cochlearium
Expression system: Escherichia coli
UniProt:
  • Canonical: P80077 (Residues: 1-483; Coverage: 100%)
Gene name: glmE
Sequence domains: Methylaspartate mutase E chain (MutE)
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 64.33Å b: 113.14Å c: 108.61Å
α: 90° β: 95.62° γ: 90°
R-values:
R R work R free
0.16 not available 0.218
Expression system: Escherichia coli