3GZ2: IpgC

Crystal structure of IpgC in complex with an IpaB peptide. Determined by X-ray diffraction at 2.65 Å resolution. Released 21 Apr 2010.

Method
X-ray diffraction
Resolution
2.65 Å
Organism
Shigella flexneri
Chains
3
Atoms
2,398
Mol. weight
42.98 kDa
Released
21 Apr 2010

Explore 3GZ2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3GZ2 contains 18 α-helices and 0 β-strands across 2 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.

Chain A: 9 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix11-2010
α-helix25-284
α-helix33-4816
α-helix52-6514
α-helix70-8314
α-helix86-9914
α-helix105-11612
α-helix120-13314
α-helix137-15014
Chain B: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix12-2110
α-helix25-284
α-helix35-4814
α-helix52-6514
α-helix70-8213
α-helix86-9813
α-helix105-11612
α-helix120-13314
α-helix137-15014

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chaperone protein ipgCA, Bprotein151Shigella flexneriP0A2U4 (AlphaFold model)
Invasin ipaBPprotein78Shigella flexneriP18011 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3GZ2_1 Chaperone protein ipgC (chains A, B)
GSLNITENESISTAVIDAINSGATLKDINAIPDDMMDDIYSYAYDFYNKGRIEEAEVFFR
FLCIYDFYNVDYIMGLAAIYQIKEQFQQAADLYAVAFALGKNDYTPVFHTGQCQLRLKAP
LKAKECFELVIQHSNDEKLKIKAQSYLDAIQ
Sequence of entity 2 (P), FASTA
>3GZ2_2 Invasin ipaB (chains P)
MGSSHHHHHHSSGLVPRGSHMILTSTELGDNTIQAANDAANKLFSLTIADLTANQNINTT
NAHSTSNILIPELKAPKS

Primary citation

Combination of two separate binding domains defines stoichiometry between type III secretion system chaperone IpgC and translocator protein IpaB. Lokareddy, R.K., Lunelli, M., Eilers, B. et al. J Biol Chem (2010) 285:39965-39975. DOI 10.1074/jbc.M110.135616 · 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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