› 2rtk

X-ray diffraction
1.82Å resolution

STREPTAVIDIN-GLYCOLURIL COMPLEX, PH 2.58, SPACE GROUP I4122 PREPARED FROM AN APOSTREPTAVIDIN CRYSTAL

Released:
DOI: 10.2210/pdb2rtk/pdb
PDB entry 2rtk coloured by chain, front view.
PDB entry 2rtk coloured by chain, side view.
PDB entry 2rtk coloured by chain, top view.
Source organism: Streptomyces avidinii
Primary publication:
Binding of biotin to streptavidin stabilizes intersubunit salt bridges between Asp61 and His87 at low pH.
Katz BA
J Mol Biol 274 776-800 (1997)
PMID: 9405158

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Streptavidin Chain: A
Molecule details ›
Chain: A
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

Ligands and Environments

3 bound ligands:
Ligand ACT 1 x ACT
Ligand SO4 1 x SO4
Ligand GLL 1 x GLL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I4122
Unit cell:
a: 58.2Å b: 58.2Å c: 176.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.276

Quick links

Citations

2 review citations

Pseudoreceptor models in drug design: bridging ligand- and receptor-based virtual screening.
Tanrikulu et al. (2008)
1 more

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)