› 3zvi

X-ray diffraction
1.9Å resolution

Methylaspartate ammonia lyase from Clostridium tetanomorphum mutant L384A

Released:
DOI: 10.2210/pdb3zvi/pdb
PDB entry 3zvi coloured by chain, front view.
PDB entry 3zvi coloured by chain, side view.
PDB entry 3zvi coloured by chain, top view.
Source organism: Clostridium tetanomorphum
Primary publication:
Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids.
Raj H, Szymański W, de Villiers J, Rozeboom HJ, Veetil VP, Reis CR, de Villiers M, Dekker FJ, de Wildeman S, Quax WJ, Thunnissen AM, Feringa BL, Janssen DB, Poelarends GJ
Nat Chem 4 478-84 (2012)
PMID: 22614383

Function and Biology Details

Reaction catalysed: 
L-threo-3-methylaspartate = mesaconate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170213 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylaspartate ammonia-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 438 amino acids
Theoretical weight: 48.45 KDa
Source organism: Clostridium tetanomorphum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05514 (Residues: 1-413; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand GOL 5 x GOL
Ligand ROP 2 x ROP
Ligand MG 2 x MG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P212121
Unit cell:
a: 66.621Å b: 109.863Å c: 110.853Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.16 0.21
Expression system: Escherichia coli

Quick links

Citations

11 review citations

New generation of biocatalysts for organic synthesis.
Nestl et al. (2014)
10 more

1 mention without citation

Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct.
Grøftehauge et al. (2015)