5jtr

Solution NMR

The structure of chaperone SecB in complex with unstructured MBP binding site e

Released:

Function and Biology Details

Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein-export protein SecB Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 155 amino acids
Theoretical weight: 17.29 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AG86 (Residues: 1-155; Coverage: 100%)
Gene names: JW3584, b3609, secB
Sequence domains: Preprotein translocase subunit SecB
Structure domains: SecB-like
Maltose/maltodextrin-binding periplasmic protein Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 40 amino acids
Theoretical weight: 4.6 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AEY0 (Residues: 168-207; Coverage: 11%)
Gene names: ECs5017, Z5632, malE

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 13%
Refinement method: molecular dynamics
Chemical shifts: BMR30086  
Expression system: Escherichia coli BL21(DE3)