› 3sey

X-ray diffraction
1.85Å resolution

Zn-mediated Polymer of Maltose-binding Protein A216H/K220H by Synthetic Symmetrization (Form II)

Released:
DOI: 10.2210/pdb3sey/pdb
PDB entry 3sey coloured by chain, front view.
PDB entry 3sey coloured by chain, side view.
PDB entry 3sey coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
An approach to crystallizing proteins by metal-mediated synthetic symmetrization.
Laganowsky A, Zhao M, Soriaga AB, Sawaya MR, Cascio D, Yeates TO
Protein Sci 20 1876-90 (2011)
PMID: 21898649

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142637 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Maltose/maltodextrin-binding periplasmic protein Chains: A, C, E
Molecule details ›
Chains: A, C, E
Length: 372 amino acids
Theoretical weight: 40.7 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-384; Coverage: 97%)
Gene names: JW3994, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
3 bound ligands:
Ligand ZN 23 x ZN
Ligand ACT 8 x ACT
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 100.66Å b: 63.65Å c: 221.83Å
α: 90° β: 90.06° γ: 90°
R-values:
R R work R free
0.21 0.208 0.247
Expression system: Escherichia coli

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Citations

9 review citations

The design of symmetric protein nanomaterials comes of age in theory and practice.
Yeates et al. (2016)
8 more