› 3rpt

X-ray diffraction
1.3Å resolution

Crystal structure of the anti-HIV b12 scaffold protein

Released:
DOI: 10.2210/pdb3rpt/pdb
PDB entry 3rpt coloured by chain, front view.
PDB entry 3rpt coloured by chain, side view.
PDB entry 3rpt coloured by chain, top view.
Source organism: Thermobifida fusca
Primary publication:
Computation-guided backbone grafting of a discontinuous motif onto a protein scaffold.
Azoitei ML, Correia BE, Ban YE, Carrico C, Kalyuzhniy O, Chen L, Schroeter A, Huang PS, McLellan JS, Kwong PD, Baker D, Strong RK, Schief WR
Science 334 373-6 (2011)
PMID: 22021856

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150674 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoglucanase E-2 Chains: A, X
Molecule details ›
Chains: A, X
Length: 282 amino acids
Theoretical weight: 29.83 KDa
Source organism: Thermobifida fusca
Expression system: Escherichia coli
UniProt:
  • Canonical: P26222 (Residues: 33-317; Coverage: 67%)
Gene name: celB
Sequence domains: Glycosyl hydrolases family 6
Structure domains: 1, 4-beta cellobiohydrolase

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P1
Unit cell:
a: 45.867Å b: 46.24Å c: 62.282Å
α: 78.57° β: 81.8° γ: 61.11°
R-values:
R R work R free
0.175 0.174 0.202
Expression system: Escherichia coli

Quick links

Citations

45 review citations

The protein-folding problem, 50 years on.
Dill et al. (2012)
44 more

2 mentions without citation

Strategies to control the binding mode of de novo designed protein interactions.
Der et al. (2013)
1 more