› 2hxx

X-ray diffraction
2Å resolution

Aminotryptophan Barstar

Released:
DOI: 10.2210/pdb2hxx/pdb
Model geometry
Fit model/data
PDB entry 2hxx coloured by chain, front view.
PDB entry 2hxx coloured by chain, side view.
PDB entry 2hxx coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Aminotryptophan-containing barstar: structure--function tradeoff in protein design and engineering with an expanded genetic code.
Rubini M, Lepthien S, Golbik R, Budisa N
Biochim Biophys Acta 1764 1147-58 (2006)
PMID: 16782415

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145869 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Barstar Chains: A, B
Molecule details ›
Chains: A, B
Length: 89 amino acids
Theoretical weight: 10.18 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11540 (Residues: 2-90; Coverage: 99%)
Sequence domains: Barstar (barnase inhibitor)
Structure domains: Barstar-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand 4IN 6 x 4IN

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2
Unit cell:
a: 85.16Å b: 46.85Å c: 51.06Å
α: 90° β: 121.34° γ: 90°
R-values:
R R work R free
0.251 0.251 0.29
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Biocatalysis with Unnatural Amino Acids: Enzymology Meets Xenobiology.
Agostini et al. (2017)
4 more

2 mentions without citation

Prospects for de novo phasing with de novo protein models.
Das et al. (2009)
1 more