X-ray diffraction
1.9Å resolution

Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design

Source organism: Finegoldia magna ATCC 29328
Primary publication:
Conversion of monomeric protein L to an obligate dimer by computational protein design.
Proc. Natl. Acad. Sci. U.S.A. 98 10687-91 (2001)
PMID: 11526208

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
GRAM_POS_ANCHORING domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 72 amino acids
Theoretical weight: 8.06 KDa
Source organism: Finegoldia magna ATCC 29328
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q51912 (Residues: 111-173; Coverage: 9%)
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 46.762Å b: 76.744Å c: 59.797Å
α: 90° β: 90° γ: 90°
R R work R free
0.193 0.193 0.218
Expression system: Escherichia coli BL21(DE3)