Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-140006 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone protein FimC
Molecule details ›
Chains: A, C, E, G, I, K, M, O
Length: 205 amino acids
Theoretical weight: 22.69 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 205 amino acids
Theoretical weight: 22.69 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P31697 (Residues: 37-241; Coverage: 100%)
Sequence domains:
- Pili and flagellar-assembly chaperone, PapD N-terminal domain
- Pili assembly chaperone PapD, C-terminal domain
Type 1 fimbrin D-mannose specific adhesin
Molecule details ›
Chains: B, D, F, H, J, L, N, P
Length: 279 amino acids
Theoretical weight: 29.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Fimbrial-type adhesion domain
Length: 279 amino acids
Theoretical weight: 29.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: P08191 (Residues: 22-300; Coverage: 100%)
Sequence domains:
Structure domains: Fimbrial-type adhesion domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE BM14
Spacegroup:
C2
Expression system: Escherichia coli
