› 7oa2

X-ray diffraction
2.7Å resolution

Triphosphate tunnel metalloenzyme from Sulfolobus acidocaldarius in complex with pyrophosphate

Released:
DOI: 10.2210/pdb7oa2/pdb
Model geometry
Fit model/data
PDB entry 7oa2 coloured by chain, front view.
PDB entry 7oa2 coloured by chain, side view.
PDB entry 7oa2 coloured by chain, top view.
Source organism: Sulfolobus acidocaldarius DSM 639
Primary publication:
The archaeal triphosphate tunnel metalloenzyme SaTTM defines structural determinants for the diverse activities in the CYTH protein family.
Vogt MS, Ngouoko Nguepbeu RR, Mohr MKF, Albers SV, Essen LO, Banerjee A
OpenAccess logo J Biol Chem 297 100820 (2021)
PMID: 34029589

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175572 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CYTH domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 198 amino acids
Theoretical weight: 23.7 KDa
Source organism: Sulfolobus acidocaldarius DSM 639
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4JAT2 (Residues: 2-185; Coverage: 100%)
Gene name: Saci_0718
Sequence domains: CYTH domain

Ligands and Environments

2 bound ligands:
Ligand POP 1 x POP
Ligand K 1 x K
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P41212
Unit cell:
a: 61.312Å b: 61.312Å c: 138.535Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.291 0.29 0.318
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes.
Bettendorff L. (2021)
2 more

1 mention without citation

The archaeal triphosphate tunnel metalloenzyme SaTTM defines structural determinants for the diverse activities in the CYTH protein family.
Vogt et al. (2021)