› 3atr

X-ray diffraction
1.8Å resolution

Geranylgeranyl Reductase (GGR) from Sulfolobus acidocaldarius co-crystallized with its ligand

Released:
DOI: 10.2210/pdb3atr/pdb
Model geometry
Fit model/data
PDB entry 3atr coloured by chain, front view.
PDB entry 3atr coloured by chain, side view.
PDB entry 3atr coloured by chain, top view.
Source organism: Sulfolobus acidocaldarius
Primary publication:
Structure and mutation analysis of archaeal geranylgeranyl reductase.
Sasaki D, Fujihashi M, Iwata Y, Murakami M, Yoshimura T, Hemmi H, Miki K
J Mol Biol 409 543-57 (2011)
PMID: 21515284

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175571 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Digeranylgeranylglycerophospholipid reductase Chain: A
Molecule details ›
Chain: A
Length: 453 amino acids
Theoretical weight: 50.83 KDa
Source organism: Sulfolobus acidocaldarius
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4JA33 (Residues: 1-452; Coverage: 100%)
Gene name: Saci_0986
Sequence domains:
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments

3 bound ligands:
Ligand FDA 1 x FDA
Ligand DD9 1 x DD9
Ligand PPV 1 x PPV
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P212121
Unit cell:
a: 62.984Å b: 82.054Å c: 105.837Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.177 0.21
Expression system: Escherichia coli

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Citations

4 review citations

Biosynthesis of archaeal membrane ether lipids.
Jain et al. (2014)
3 more

3 mentions without citation

The Chinese hamster dihydrofolate reductase replication origin beta is active at multiple ectopic chromosomal locations and requires specific DNA sequence elements for activity.
Altman et al. (2001)
2 more