› 5hi1

X-ray diffraction
2.15Å resolution

Backbone Modifications in the Protein GB1 Helix: Aib24, beta-3-Lys28, beta-3-Lys31, Aib35

Released:
DOI: 10.2210/pdb5hi1/pdb
PDB entry 5hi1 coloured by chain, front view.
PDB entry 5hi1 coloured by chain, side view.
PDB entry 5hi1 coloured by chain, top view.
Source organism: Streptococcus sp. 'group G'
Primary publication:
Comparison of design strategies for α-helix backbone modification in a protein tertiary fold.
Tavenor NA, Reinert ZE, Lengyel GA, Griffith BD, Horne WS
Chem Commun (Camb) 52 3789-92 (2016)
PMID: 26853882

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148791 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Immunoglobulin G-binding protein G Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 57 amino acids
Theoretical weight: 6.19 KDa
Source organism: Streptococcus sp. 'group G'
Expression system: Not provided
UniProt:
  • Canonical: P19909 (Residues: 302-357; Coverage: 10%)
Gene name: spg
Sequence domains: B domain
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

1 bound ligand:
Ligand ACT 2 x ACT
2 modified residues:
Ligand AIB 16 x AIB
Ligand B3K 16 x B3K

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 74.371Å b: 73.43Å c: 79.436Å
α: 90° β: 99.35° γ: 90°
R-values:
R R work R free
0.217 0.214 0.252
Expression system: Not provided

Quick links

Citations

3 review citations

Systematic Targeting of Protein-Protein Interactions.
Modell et al. (2016)
2 more

4 mentions without citation

Foldamer Tertiary Structure through Sequence-Guided Protein Backbone Alteration.
George et al. (2018)
3 more