PDBe 1kr5

X-ray diffraction
2.1Å resolution

Crystal structure of human L-isoaspartyl methyltransferase

Released:
Source organism: Homo sapiens

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-L-isoaspartate(D-aspartate) O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 226 amino acids
Theoretical weight: 24.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22061 (Residues: 2-227; Coverage: 100%)
Gene name: PCMT1
Sequence domains: Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P21
Unit cell:
a: 48.007Å b: 53.698Å c: 49.003Å
α: 90° β: 115.6° γ: 90°
R-values:
R R work R free
0.224 0.221 0.264
Expression system: Escherichia coli