1jg3

X-ray diffraction
2.1Å resolution

Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with adenosine & VYP(ISP)HA substrate

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-162260 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein-L-isoaspartate O-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 235 amino acids
Theoretical weight: 26.61 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TZR3 (Residues: 1-219; Coverage: 100%)
Gene names: PF1922, pcm
Sequence domains: Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)
Structure domains: Vaccinia Virus protein VP39
VYP(L-iso-ASP)HA Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 702 Da
Source organism: Pyrococcus furiosus
Expression system: Not provided

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D
Spacegroup: P61
Unit cell:
a: 91.573Å b: 91.573Å c: 124.547Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.204 0.233
Expression systems:
  • Escherichia coli
  • Not provided