› 2lxy

Solution NMR

NMR structure of 2-MERCAPTOPHENOL-ALPHA3C

Released:
DOI: 10.2210/pdb2lxy/pdb
PDB entry 2lxy coloured by chain, ensemble of 32 models, front view.
PDB entry 2lxy coloured by chain, ensemble of 32 models, side view.
PDB entry 2lxy coloured by chain, ensemble of 32 models, top view.
Source organism: Synthetic construct
Primary publication:
Reversible phenol oxidation and reduction in the structurally well-defined 2-Mercaptophenol-α₃C protein.
Tommos C, Valentine KG, Martínez-Rivera MC, Liang L, Moorman VR
Biochemistry 52 1409-18 (2013)
PMID: 23373469

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-162938 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-mercaptophenol-alpha3C Chain: A
Molecule details ›
Chain: A
Length: 67 amino acids
Theoretical weight: 7.48 KDa
Source organism: Synthetic construct
Expression system: Escherichia coli
Structure domains: Designed single chain three-helix bundle

Ligands and Environments

1 bound ligand:
Ligand HTS 1 x HTS
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 93%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Designed for life: biocompatible de novo designed proteins and components.
Grayson et al. (2018)
1 more

6 mentions without citation

Near UV-Visible electronic absorption originating from charged amino acids in a monomeric protein.
Prasad et al. (2017)
5 more