› 4wva

X-ray diffraction
1.67Å resolution

Crystal structure of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8 in complex with Tris

Released:
DOI: 10.2210/pdb4wva/pdb
PDB entry 4wva coloured by chain, front view.
PDB entry 4wva coloured by chain, side view.
PDB entry 4wva coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Crystal structure and substrate-binding mode of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8.
Miyazaki T, Ichikawa M, Iino H, Nishikawa A, Tonozuka T
J Struct Biol 190 21-30 (2015)
PMID: 25712767

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-562249 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannosylglycerate hydrolase MGH1-like glycoside hydrolase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 420 amino acids
Theoretical weight: 48.84 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SJN0 (Residues: 1-420; Coverage: 100%)
Gene name: TTHA0978
Sequence domains: Mannosylglycerate hydrolase MGH1-like glycoside hydrolase domain
Structure domains: Glycosyltransferase

Ligands and Environments

3 bound ligands:
Ligand CL 2 x CL
Ligand TRS 2 x TRS
Ligand MPD 5 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: R3
Unit cell:
a: 92.01Å b: 92.01Å c: 267.235Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.147 0.146 0.173
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Mannoside recognition and degradation by bacteria.
Ladevèze et al. (2017)
2 other articles

1 mention without citation

The structural characterization of a glucosylglycerate hydrolase provides insights into the molecular mechanism of mycobacterial recovery from nitrogen starvation.
Cereija et al. (2019)