› 4pin

X-ray diffraction
1.9Å resolution

Ergothioneine-biosynthetic methyltransferase EgtD in complex with N,N-dimethylhistidine

Released:
DOI: 10.2210/pdb4pin/pdb
PDB entry 4pin coloured by chain, front view.
PDB entry 4pin coloured by chain, side view.
PDB entry 4pin coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis
Primary publication:
Ergothioneine biosynthetic methyltransferase EgtD reveals the structural basis of aromatic amino acid betaine biosynthesis.
Vit A, Misson L, Blankenfeldt W, Seebeck FP
Chembiochem 16 119-25 (2015)
PMID: 25404173

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + L-histidine = S-adenosyl-L-homocysteine + N(alpha)-methyl-L-histidine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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: 323 amino acids
Theoretical weight: 35.28 KDa
Source organism: Mycolicibacterium smegmatis
Expression system: Escherichia coli BL21(DE3)
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:
Ligand AVI 2 x AVI
Ligand PO4 5 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 71.988Å b: 74.757Å c: 137.812Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.241
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

The biology of ergothioneine, an antioxidant nutraceutical.
Borodina et al. (2020)
3 more