PDBe 3iei

X-ray diffraction
1.9Å resolution

Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine

Released:
Source organism: Homo sapiens
Entry authors: Xing Y, Jeffry PD

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine carboxyl methyltransferase 1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 334 amino acids
Theoretical weight: 38.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UIC8 (Residues: 1-334; Coverage: 100%)
  • Best match: Q9UIC8-2 (Residues: 60-357)
Gene names: CGI-68, LCMT, LCMT1
Sequence domains: Leucine carboxyl methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 8 x SAH
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P1
Unit cell:
a: 106.036Å b: 81.127Å c: 82.816Å
α: 105.41° β: 93.97° γ: 104.29°
R-values:
R R work R free
0.186 0.184 0.232
Expression system: Escherichia coli