Function and Biology Details
Reaction catalysed:
L-threo-3-methylaspartate = L-glutamate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Glutamate mutase sigma subunit (preferred)
PDBe Complex ID:
PDB-CPX-160346 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate mutase sigma subunit
Molecule details ›
Chain: A
Length: 137 amino acids
Theoretical weight: 14.83 KDa
Source organism: Clostridium cochlearium
Expression system: Escherichia coli
UniProt:
Sequence domains: B12 binding domain
Structure domains: Cobalamin-binding domain
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%)
Sequence domains: B12 binding domain
Structure domains: Cobalamin-binding domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
DISTANCE GEOMETRY, SIMULATED ANNEALING, ENERGY MINIMIZATION
Expression system: Escherichia coli
