› 1ls1

X-ray diffraction
1.1Å resolution

T. aquaticus Ffh NG Domain at 1.1A Resolution

Released:
DOI: 10.2210/pdb1ls1/pdb
PDB entry 1ls1 coloured by chain, front view.
PDB entry 1ls1 coloured by chain, side view.
PDB entry 1ls1 coloured by chain, top view.
Source organism: Thermus aquaticus
Primary publication:
Structural basis for mobility in the 1.1 A crystal structure of the NG domain of Thermus aquaticus Ffh.
Ramirez UD, Minasov G, Focia PJ, Stroud RM, Walter P, Kuhn P, Freymann DM
J Mol Biol 320 783-99 (2002)
PMID: 12095255

Function and Biology Details

Reaction catalysed: 
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126575 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Signal recognition particle protein Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 32.36 KDa
Source organism: Thermus aquaticus
Expression system: Escherichia coli
UniProt:
  • Canonical: O07347 (Residues: 1-295; Coverage: 69%)
Gene name: ffh
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand OXY 3 x OXY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: C2
Unit cell:
a: 99.734Å b: 53.675Å c: 57.836Å
α: 90° β: 119.92° γ: 90°
R-values:
R R work R free
0.137 0.135 0.168
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Structure, function and evolution of the signal recognition particle.
Nagai et al. (2003)
3 more

10 mentions without citation

Detecting evolutionary relationships across existing fold space, using sequence order-independent profile-profile alignments.
Xie et al. (2008)
9 more