› 4zfk

X-ray diffraction
1.82Å resolution

Ergothioneine-biosynthetic Ntn hydrolase EgtC with glutamine

Released:
DOI: 10.2210/pdb4zfk/pdb
PDB entry 4zfk coloured by chain, front view.
PDB entry 4zfk coloured by chain, side view.
PDB entry 4zfk coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis MC2 155
Primary publication:
Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC.
Vit A, Mashabela GT, Blankenfeldt W, Seebeck FP
Chembiochem 16 1490-6 (2015)
PMID: 26079795

Function and Biology Details

Reaction catalysed: 
Gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H(2)O = S-(hercyn-2-yl)-L-cysteine S-oxide + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106469 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 235 amino acids
Theoretical weight: 25.24 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0R5M9 (Residues: 1-227; Coverage: 100%)
Gene names: MSMEG_6248, MSMEI_6087, egtC
Sequence domains: Glutamine amidotransferases class-II
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

Ligands and Environments

2 bound ligands:
Ligand EDO 27 x EDO
Ligand GLN 4 x GLN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 61.796Å b: 109.993Å c: 139.327Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.146 0.176
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