3kdz

X-ray diffraction
2.2Å resolution

X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand

Released:

Function and Biology Details

Reactions catalysed:
L-tyrosine = trans-p-hydroxycinnamate + ammonia
L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-184536 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MIO-dependent tyrosine 2,3-aminomutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 537 amino acids
Theoretical weight: 58.15 KDa
Source organism: Streptomyces globisporus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8GMG0 (Residues: 1-539; Coverage: 100%)
Sequence domains: Aromatic amino acid lyase
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21212
Unit cell:
a: 92.722Å b: 145.941Å c: 74.812Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.205 0.249
Expression system: Escherichia coli