› 3o7w

X-ray diffraction
2Å resolution

The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1

Released:
DOI: 10.2210/pdb3o7w/pdb
PDB entry 3o7w coloured by chain, front view.
PDB entry 3o7w coloured by chain, side view.
PDB entry 3o7w coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.
Tsai ML, Cronin N, Djordjevic S
Acta Crystallogr D Biol Crystallogr 67 14-24 (2011)
PMID: 21206058

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine = S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193781 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine carboxyl methyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 33.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UIC8 (Residues: 23-232, 259-334; Coverage: 86%)
Gene names: CGI-68, LCMT, LCMT1
Sequence domains: Leucine carboxyl methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAM 1 x SAM
2 bound ligands:
Ligand GOL 1 x GOL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 49.086Å b: 63.296Å c: 81.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.265
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity.
Sents et al. (2013)
5 other articles