1KFM: Major outer membrane lipoprotein

Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants. Determined by X-ray diffraction at 2.0 Å resolution. Released 28 Jun 2002.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Escherichia coli
Chains
1
Atoms
382
Mol. weight
6.07 kDa
Released
28 Jun 2002

Explore 1KFM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KFM contains 1 α-helix 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: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix3-4947

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Major outer membrane lipoproteinAprotein56Escherichia coliP69776 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1KFM_1 MAJOR OUTER MEMBRANE LIPOPROTEIN (chains A)
SSNAKIDQLSSDVQTLNAKVDQLSNDVNAARSDAQAAKDDAARANQRLDNMATKYR

Primary citation

Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants. Liu, J., Cao, W., Lu, M. J Mol Biol (2002) 318:877-888. DOI 10.1016/S0022-2836(02)00138-9 · PubMed

Other PDB entries of the same protein (UniProt P69776 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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