› 1slg

X-ray diffraction
1.76Å resolution

STREPTAVIDIN, PH 5.6, BOUND TO PEPTIDE FCHPQNT

Released:
DOI: 10.2210/pdb1slg/pdb
PDB entry 1slg coloured by chain, front view.
PDB entry 1slg coloured by chain, side view.
PDB entry 1slg coloured by chain, top view.
Source organism: Streptomyces avidinii
Primary publication:
Binding to protein targets of peptidic leads discovered by phage display: crystal structures of streptavidin-bound linear and cyclic peptide ligands containing the HPQ sequence.
Katz BA
Biochemistry 34 15421-9 (1995)
PMID: 7492542

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-149706 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Streptavidin Chains: B, D
Molecule details ›
Chains: B, D
Length: 135 amino acids
Theoretical weight: 14.18 KDa
Source organism: Streptomyces avidinii
UniProt:
  • Canonical: P22629 (Residues: 25-159; Coverage: 85%)
Sequence domains: Avidin family
Structure domains: Avidin-like
FCHPQNT Chains: M, P
Molecule details ›
Chains: M, P
Length: 7 amino acids
Theoretical weight: 831 Da
Source organism: Streptomyces avidinii

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 96.24Å b: 105.89Å c: 48.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.222

Quick links

Citations

11 review citations

Selection-based discovery of druglike macrocyclic peptides.
Passioura et al. (2014)
10 more

4 mentions 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)
3 more