3ks2

X-ray diffraction
3.3Å resolution

Crystal Structure of Type-III Secretion Chaperone IpgC from Shigella flexneri (residues 10-155)

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141073 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein IpgC Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
Length: 151 amino acids
Theoretical weight: 17.13 KDa
Source organism: Shigella flexneri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A2U4 (Residues: 10-155; Coverage: 94%)
Gene names: CP0129, ipgC, ippI
Sequence domains: Tetratricopeptide repeat
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P21
Unit cell:
a: 140.496Å b: 71.474Å c: 171.012Å
α: 90° β: 93.86° γ: 90°
R-values:
R R work R free
0.26 0.259 0.296
Expression system: Escherichia coli BL21(DE3)