› 2nrq

X-ray diffraction
2.6Å resolution

Crystal structure of protein SSO0741 from Sulfolobus solfataricus, Pfam DUF54

Released:
DOI: 10.2210/pdb2nrq/pdb
PDB entry 2nrq coloured by chain, front view.
PDB entry 2nrq coloured by chain, side view.
PDB entry 2nrq coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
UPF201 archaeal specific family members reveal structural similarity to RNA-binding proteins but low likelihood for RNA-binding function.
Rao KN, Burley SK, Swaminathan S
PLoS One 3 e3903 (2008)
PMID: 19079550

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194124 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-binding protein Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.75 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UXC9 (Residues: 2-149; Coverage: 99%)
Gene names: HFC64_15305, ORF-c20_032, SSOP1_0766, SULA_1824, SULB_1825, SULC_1823, SULG_09155, SULH_09155, SULI_09155, SULM_09145, SULN_09145, SULO_09155, SULZ_09080
Sequence domains: RNA binding
Structure domains: 50s Ribosomal Protein L5; Chain: A,

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: R32
Unit cell:
a: 127.54Å b: 127.54Å c: 61.64Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.245 0.245 0.303
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135.
Luz et al. (2010)

1 mention without citation

UPF201 archaeal specific family members reveal structural similarity to RNA-binding proteins but low likelihood for RNA-binding function.
Rao et al. (2008)