› 1id8

Solution NMR

NMR STRUCTURE OF GLUTAMATE MUTASE (B12-BINDING SUBUNIT) COMPLEXED WITH THE VITAMIN B12 NUCLEOTIDE

Released:
DOI: 10.2210/pdb1id8/pdb
PDB entry 1id8 coloured by chain, ensemble of 15 models, front view.
PDB entry 1id8 coloured by chain, ensemble of 15 models, side view.
PDB entry 1id8 coloured by chain, ensemble of 15 models, top view.
Source organism: Clostridium tetanomorphum
Primary publication:
The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12).
Tollinger M, Eichmüller C, Konrat R, Huhta MS, Marsh EN, Kräutler B
J Mol Biol 309 777-91 (2001)
PMID: 11397096

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 BL21(DE3)
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

2 bound ligands:
Ligand FOP 1 x FOP
Ligand DBI 1 x DBI
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: restrained simulated annealing, molecular dynamics, energy minimazation
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Vitamin B12-derivatives-enzyme cofactors and ligands of proteins and nucleic acids.
Gruber et al. (2011)
2 more