2yh5

X-ray diffraction
1.25Å resolution

Structure of the C-terminal domain of BamC

Released:
Source organism: Escherichia coli K-12
Primary publication:
Structural basis of outer membrane protein biogenesis in bacteria.
J Biol Chem 286 27792-803 (2011)
PMID: 21586578

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-141761 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane protein assembly factor BamC Chain: A
Molecule details ›
Chain: A
Length: 127 amino acids
Theoretical weight: 13.9 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A903 (Residues: 226-344; Coverage: 37%)
Gene names: JW2462, b2477, bamC, dapX, nlpB
Sequence domains: NlpB/DapX lipoprotein
Structure domains: Outer membrane protein assembly factor BamC

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 29.74Å b: 59.12Å c: 31.06Å
α: 90° β: 116.37° γ: 90°
R-values:
R R work R free
0.148 0.146 0.184
Expression system: Escherichia coli BL21(DE3)