› 1vwf

X-ray diffraction
1.92Å resolution

STREPTAVIDIN COMPLEXED WITH CYCLO-AC-[CHPQGPPC]-NH2 MONOMER, PH 3.67

Released:
DOI: 10.2210/pdb1vwf/pdb
PDB entry 1vwf coloured by chain, front view.
PDB entry 1vwf coloured by chain, side view.
PDB entry 1vwf coloured by chain, top view.
Source organism: Streptomyces avidinii
Primary publication:
In crystals of complexes of streptavidin with peptide ligands containing the HPQ sequence the pKa of the peptide histidine is less than 3.0.
Katz BA, Cass RT
J Biol Chem 272 13220-8 (1997)
PMID: 9148939

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149714 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Streptavidin Chain: B
Molecule details ›
Chain: B
Length: 123 amino acids
Theoretical weight: 12.97 KDa
Source organism: Streptomyces avidinii
Expression system: Not provided
UniProt:
  • Canonical: P22629 (Residues: 37-159; Coverage: 77%)
Sequence domains: Avidin family
Structure domains: Avidin-like
PEPTIDE LIGAND CONTAINING HPQ Chain: P
Molecule details ›
Chain: P
Length: 10 amino acids
Theoretical weight: 863 Da
Source organism: Streptomyces avidinii
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I4122
Unit cell:
a: 59.53Å b: 59.53Å c: 179.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.236
Expression system: Not provided

Quick links

Citations

1 review citation

Streptavidin-binding and -dimerizing ligands discovered by phage display, topochemistry, and structure-based design.
Katz BA. (1999)
13 other articles

1 mention without citation

Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site.
Korndörfer et al. (2002)