› 2xz3

X-ray diffraction
1.95Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Envelope glycoprotein; Maltose/maltodextrin-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 463 amino acids
Theoretical weight: 51.21 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AEX9 (Residues: 27-392; Coverage: 99%)
  • Canonical: Q90M13 (Residues: 326-418; Coverage: 18%)
Gene names: JW3994, b4034, env, malE
Sequence domains: Bacterial extracellular solute-binding protein

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand EDO 6 x EDO
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: R3
Unit cell:
a: 107.595Å b: 107.595Å c: 119.17Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.192 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Why continuum electrostatics theories cannot explain biological structure, polyelectrolytes or ionic strength effects in ion-protein interactions.
Collins KD. (2012)
3 more

4 mentions without citation

Crystal structures of MBP fusion proteins.
Waugh DS. (2016)
3 more