› 3csg

X-ray diffraction
1.8Å resolution

Crystal Structure of Monobody YS1(MBP-74)/Maltose Binding Protein Fusion Complex

Released:
DOI: 10.2210/pdb3csg/pdb
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Source organism: Escherichia coli
Primary publication:
A dominant conformational role for amino acid diversity in minimalist protein-protein interfaces.
Gilbreth RN, Esaki K, Koide A, Sidhu SS, Koide S
J Mol Biol 381 407-18 (2008)
PMID: 18602117

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Maltose/maltodextrin-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 461 amino acids
Theoretical weight: 50.5 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 31-396; Coverage: 99%)
Gene names: JW3994, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P41
Unit cell:
a: 68.578Å b: 68.578Å c: 108.002Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.187 0.235
Expression system: Escherichia coli

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Citations

14 review citations

Engineered protein scaffolds as next-generation antibody therapeutics.
Gebauer et al. (2009)
13 more

7 mentions without citation

The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins.
Koide et al. (2009)
6 more

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