› 5n8w

X-ray diffraction
1.1Å resolution

CRYSTAL STRUCTURE OF STREPTAVIDIN with D-amino acid containing peptide GGwhdeatwkpG

Released:
DOI: 10.2210/pdb5n8w/pdb
PDB entry 5n8w coloured by chain, front view.
PDB entry 5n8w coloured by chain, side view.
PDB entry 5n8w coloured by chain, top view.
Source organisms:
Primary publication:
Stepwise Evolution Improves Identification of Diverse Peptides Binding to a Protein Target.
Lyamichev VI, Goodrich LE, Sullivan EH, Bannen RM, Benz J, Albert TJ, Patel JJ
Sci Rep 7 12116 (2017)
PMID: 28935886

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149734 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Streptavidin Chains: A, B
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 18.85 KDa
Source organism: Streptomyces avidinii
Expression system: Escherichia coli
UniProt:
  • Canonical: P22629 (Residues: 1-183; Coverage: 100%)
Sequence domains: Avidin family
Structure domains: Avidin-like
GLY-GLY-DTR-DHI-DAS-DGL-DAL-DTH-DTR-DLY Chains: C, D
Molecule details ›
Chains: C, D
Length: 14 amino acids
Theoretical weight: 1.62 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
8 modified residues:
Ligand DTR 4 x DTR
Ligand DHI 2 x DHI
Ligand DAS 2 x DAS
Ligand DGL 2 x DGL
Ligand DAL 2 x DAL
Ligand DTH 2 x DTH
Ligand DLY 2 x DLY
Ligand DPR 2 x DPR

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 81.882Å b: 95.72Å c: 82.059Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.136 0.135 0.151
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

New Immunoinformatics Tools for Swine: Designing Epitope-Driven Vaccines, Predicting Vaccine Efficacy, and Making Vaccines on Demand.
Moise et al. (2020)
1 more