3KS2: Chaperone protein ipgC

Crystal Structure of Type-III Secretion Chaperone IpgC from Shigella flexneri (residues 10-155). Determined by X-ray diffraction at 3.3 Å resolution. Released 25 Aug 2010.

Method
X-ray diffraction
Resolution
3.3 Å
Organism
Shigella flexneri
Chains
18
Atoms
20,052
Mol. weight
308.33 kDa
Released
25 Aug 2010

Explore 3KS2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3KS2 contains 126 α-helices and 0 β-strands across 18 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q and R: 7 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix33-4816
α-helix52-6514
α-helix70-8213
α-helix86-9813
α-helix105-11612
α-helix120-13314
α-helix137-15115

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chaperone protein ipgCA, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, Rprotein151Shigella flexneriP0A2U4 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R), FASTA
>3KS2_1 Chaperone protein ipgC (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R)
GSTGSSISTAVIDAINSGATLKDINAIPDDMMDDIYSYAYDFYNKGRIEEAEVFFRFLCI
YDFYNVDYIMGLAAIYQIKEQFQQAADLYAVAFALGKNDYTPVFHTGQCQLRLKAPLKAK
ECFELVIQHSNDEKLKIKAQSYLDAIQDIKE

Primary citation

Evidence for alternative quaternary structure in a bacterial Type III secretion system chaperone. Barta, M.L., Zhang, L., Picking, W.L. et al. BMC Struct Biol (2010) 10:21-21. DOI 10.1186/1472-6807-10-21 · PubMed

Other PDB entries of the same protein (UniProt P0A2U4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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