4uy5

X-ray diffraction
2Å resolution

Crystal structure of Histidine-specific methyltransferase EgtD from Mycobacterium smegmatis

Released:
Source organism: Mycolicibacterium smegmatis
Primary publication:
Structural insights into the histidine trimethylation activity of EgtD from Mycobacterium smegmatis.
Biochem Biophys Res Commun 452 1098-103 (2014)
PMID: 25251321

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-106468 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidine N-alpha-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 36.35 KDa
Source organism: Mycolicibacterium smegmatis
Expression system: Escherichia coli B
UniProt:
  • Canonical: A0R5M8 (Residues: 1-321; Coverage: 100%)
Gene names: MSMEG_6247, MSMEI_6086, egtD
Sequence domains: Histidine-specific methyltransferase, SAM-dependent
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P41212
Unit cell:
a: 74.641Å b: 74.641Å c: 139.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.195 0.241
Expression system: Escherichia coli B