4uy7

X-ray diffraction
2.31Å resolution

Crystal structure of Histidine bound 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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 328 amino acids
Theoretical weight: 35.98 KDa
Source organism: Mycolicibacterium smegmatis
Expression system: Escherichia coli B
UniProt:
  • Canonical: A0R5M8 (Residues: 2-321; 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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P41
Unit cell:
a: 74.499Å b: 74.499Å c: 138.954Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.192 0.247
Expression system: Escherichia coli B