› 1be1

Solution NMR

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

Released:
DOI: 10.2210/pdb1be1/pdb
PDB entry 1be1 coloured by chain, front view.
PDB entry 1be1 coloured by chain, side view.
PDB entry 1be1 coloured by chain, top view.
Source organism: Clostridium tetanomorphum
Primary publication:
How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum.
Tollinger M, Konrat R, Hilbert BH, Marsh EN, Kräutler B
Structure 6 1021-33 (1998)
PMID: 9739092

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:
PDBe Complex ID:
PDB-CPX-170208 (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-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

Quick links

Citations

3 review citations

Coenzyme B(12) dependent glutamate mutase.
Gruber et al. (2002)
2 more

1 mention without citation

Contribution to the prediction of the fold code: application to immunoglobulin and flavodoxin cases.
Banach et al. (2015)