Function and Biology Details
Biochemical function:
- not assigned
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180521 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pili assembly chaperone N-terminal domain-containing protein
Molecule details ›
Chains: A, C
Length: 243 amino acids
Theoretical weight: 27 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Pili and flagellar-assembly chaperone, PapD N-terminal domain
Length: 243 amino acids
Theoretical weight: 27 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q6XBY4 (Residues: 35-277; Coverage: 88%)
Sequence domains: Pili and flagellar-assembly chaperone, PapD N-terminal domain
Spore coat protein U domain-containing protein
Molecule details ›
Chains: B, D
Length: 152 amino acids
Theoretical weight: 15.93 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Spore Coat Protein U domain
Length: 152 amino acids
Theoretical weight: 15.93 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q6XBY7 (Residues: 38-180; Coverage: 92%)
Sequence domains: Spore Coat Protein U domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID23-1
Spacegroup:
P6522
Expression system: Escherichia coli BL21
