PDBe 1be1

Solution NMR

GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE

Released:

Function and Biology Details

Reaction catalysed:
L-threo-3-methylaspartate = L-glutamate. 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate mutase sigma subunit Chain: A
Molecule details ›
Chain: A
Length: 137 amino acids
Theoretical weight: 14.76 KDa
Source organism: Clostridium tetanomorphum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05488 (Residues: 1-137; Coverage: 100%)
Gene names: glmS, mutS
Sequence domains: B12 binding domain
Structure domains: Cobalamin (vitamin B12)-binding domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY, SIMULATED ANNEALING, ENERGY MINIMIZATION
Expression system: Escherichia coli