› 1yyx

Solution NMR

The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) at 2.8M urea

Released:
DOI: 10.2210/pdb1yyx/pdb
PDB entry 1yyx coloured by chain, ensemble of 15 models, front view.
PDB entry 1yyx coloured by chain, ensemble of 15 models, side view.
PDB entry 1yyx coloured by chain, ensemble of 15 models, top view.
Source organism: Homo sapiens
Primary publication:
Detection and structure determination of an equilibrium unfolding intermediate of Rd-apocytochrome b562: native fold with non-native hydrophobic interactions.
Feng H, Vu ND, Bai Y
J Mol Biol 343 1477-85 (2004)
PMID: 15491625

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-162584 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Redesigned apo-cytochrome b562 Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 11.73 KDa
Source organism: Homo sapiens
Expression system: Not provided
Structure domains: Cytochrome c/b562

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing, molecular dynamics, matrix relaxation, torsion angle dynamics
Expression system: Not provided

Quick links

Citations

3 review citations

The folding of single domain proteins--have we reached a consensus?
Sosnick et al. (2011)
2 more

2 mentions without citation

Fusion partner toolchest for the stabilization and crystallization of G protein-coupled receptors.
Chun et al. (2012)
1 more