› 5lo2

Solution NMR

Engineering protein stability with atomic precision in a monomeric miniprotein

Released:
DOI: 10.2210/pdb5lo2/pdb
PDB entry 5lo2 coloured by chain, ensemble of 20 models, front view.
PDB entry 5lo2 coloured by chain, ensemble of 20 models, side view.
PDB entry 5lo2 coloured by chain, ensemble of 20 models, top view.
Source organism: Streptococcus mutans
Primary publication:
Engineering protein stability with atomic precision in a monomeric miniprotein.
Baker EG, Williams C, Hudson KL, Bartlett GJ, Heal JW, Porter Goff KL, Sessions RB, Crump MP, Woolfson DN
Nat Chem Biol 13 764-770 (2017)
PMID: 28530710

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-540504 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cell surface antigen I Chain: A
Molecule details ›
Chain: A
Length: 36 amino acids
Theoretical weight: 3.81 KDa
Source organism: Streptococcus mutans
Expression system: Not provided
UniProt:
  • Canonical: P23504 (Residues: 452-470; Coverage: 1%)
Gene names: SMU_610, spaP
Sequence domains: Streptococcal surface antigen repeat

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 64%
Expression system: Not provided

Quick links

Citations

3 review citations

Secondary Forces in Protein Folding.
Newberry et al. (2019)
2 more

2 mentions without citation

The Realm of Unconventional Noncovalent Interactions in Proteins: Their Significance in Structure and Function.
Adhav et al. (2023)
1 more