2FM9: Salmonella SipA residues 48-264

Structure of Salmonella SipA residues 48-264. Determined by X-ray diffraction at 2.0 Å resolution. Released 21 Mar 2006.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Salmonella typhimurium
Chains
1
Atoms
1,633
Mol. weight
23.58 kDa
Released
21 Mar 2006

Explore 2FM9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2FM9 contains 12 α-helices and 0 β-strands across 1 chain. 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: 12 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix51-533
α-helix55-6814
α-helix73-8210
α-helix86-10520
α-helix110-13021
α-helix146-16520
α-helix168-17811
α-helix179-1835
α-helix184-19512
α-helix198-2003
α-helix201-22727
α-helix245-25814

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cell invasion protein sipAAprotein215Salmonella typhimuriumP0CL52 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2FM9_1 Cell invasion protein sipA (chains A)
PQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNNVAGKKAIMEFAGLFRSALNATSD
SPEAKTLLMKVGAEYTAQIIKDGLKEKSAFGPWLPETKKAEAKLENLEKQLLDIIKNNTG
GELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPLTRSNLTHLVDKAAAKAVEALDMCHQK
LTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPA

Primary citation

A common structural motif in the binding of virulence factors to bacterial secretion chaperones. Lilic, M., Vujanac, M., Stebbins, C.E. Mol Cell (2006) 21:653-664. DOI 10.1016/j.molcel.2006.01.026 · PubMed

Other PDB entries of the same protein (UniProt P0CL52 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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