› 3n4y

X-ray diffraction
2.4Å resolution

Crystal structure of wild-type T. celer L30e in low ionic strength condition without precipitant

Released:
DOI: 10.2210/pdb3n4y/pdb
PDB entry 3n4y coloured by chain, front view.
PDB entry 3n4y coloured by chain, side view.
PDB entry 3n4y coloured by chain, top view.
Source organism: Thermococcus celer
Primary publication:
Electrostatic contribution of surface charge residues to the stability of a thermophilic protein: benchmarking experimental and predicted pKa values.
Chan CH, Wilbanks CC, Makhatadze GI, Wong KB
PLoS One 7 e30296 (2012)
PMID: 22279578

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151359 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Large ribosomal subunit protein eL30 Chain: A
Molecule details ›
Chain: A
Length: 101 amino acids
Theoretical weight: 10.98 KDa
Source organism: Thermococcus celer
Expression system: Escherichia coli
UniProt:
  • Canonical: P29160 (Residues: 1-101; Coverage: 100%)
Gene names: rpl30, rpl30e
Sequence domains: Ribosomal protein L7Ae/L30e/S12e/Gadd45 family
Structure domains: 60s Ribosomal Protein L30; Chain: A;

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 24.179Å b: 53.307Å c: 33.733Å
α: 90° β: 109.12° γ: 90°
R-values:
R R work R free
0.187 0.177 0.278
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Therapeutic protein aggregation: mechanisms, design, and control.
Roberts CJ. (2014)
1 more

1 mention without citation

Electrostatic contribution of surface charge residues to the stability of a thermophilic protein: benchmarking experimental and predicted pKa values.
Chan et al. (2012)