› 4pwy

X-ray diffraction
1.9Å resolution

Crystal structure of a Calmodulin-lysine N-methyltransferase fragment

Released:
DOI: 10.2210/pdb4pwy/pdb
PDB entry 4pwy coloured by chain, front view.
PDB entry 4pwy coloured by chain, side view.
PDB entry 4pwy coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Tempel W, Hong BS, Walker JR, Li Y, Bountra C, Arrowsmith CH, Edwards AM, Brown PJ, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + calmodulin L-lysine = S-adenosyl-L-homocysteine + calmodulin N(6)-methyl-L-lysine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin-lysine N-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 264 amino acids
Theoretical weight: 30.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7Z624 (Residues: 61-323; Coverage: 81%)
Gene names: C2orf34, CAMKMT, CLNMT
Sequence domains: Lysine methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
3 bound ligands:
Ligand GOL 2 x GOL
Ligand UNX 19 x UNX
Ligand MLI 1 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P41212
Unit cell:
a: 80.935Å b: 80.935Å c: 121.952Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.191
Expression system: Escherichia coli

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