› 1t43

X-ray diffraction
3.2Å resolution

Crystal Structure Analysis of E.coli Protein (N5)-Glutamine Methyltransferase (HemK)

Released:
DOI: 10.2210/pdb1t43/pdb
PDB entry 1t43 coloured by chain, front view.
PDB entry 1t43 coloured by chain, side view.
PDB entry 1t43 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase.
Yang Z, Shipman L, Zhang M, Anton BP, Roberts RJ, Cheng X
J Mol Biol 340 695-706 (2004)
PMID: 15223314

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142258 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Release factor glutamine methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 31.01 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ACC1 (Residues: 1-277; Coverage: 100%)
Gene names: JW1203, b1212, hemK, prmC
Sequence domains:
Structure domains:

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 X25
Spacegroup: P63
Unit cell:
a: 138.933Å b: 138.933Å c: 40.583Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.289 0.289 0.315
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structural and sequence motifs of protein (histone) methylation enzymes.
Cheng et al. (2005)
2 more

11 mentions without citation

Natural history of S-adenosylmethionine-binding proteins.
Kozbial et al. (2005)
10 more