2KP2: Protein disulfide-isomerase

Solution structure of the b' domain of thermophilic fungal protein disulfide isomerase. Determined by solution NMR. Released 27 Oct 2009.

Method
Solution NMR
Organism
Humicola insolens
Chains
1
Atoms
1,025
Mol. weight
14.51 kDa
Released
27 Oct 2009

Explore 2KP2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2KP2 contains 7 α-helices and 5 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: 7 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand8-1031
α-helix16-205
β-strand26-3161
α-helix37-4913
β-strand56-6161
α-helix66-683
α-helix69-724
β-strand81-8551
β-strand92-9431
α-helix95-962
α-helix103-11513
α-helix128-1303

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein disulfide-isomeraseAprotein133Humicola insolensP55059 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KP2_1 Protein disulfide-isomerase (chains A)
GPLGSPLIGEIGPETYSDYMSAGIPLAYIFAETAEERKELSDKLKPIAEAQRGVINFGTI
DAKAFGAHAGNLNLKTDKFPAFAIQEVAKNQKFPFDQEKEITFEAIKAFVDDFVAGKIEP
SIKSEPIPEKQEG

Primary citation

Redox-Dependent Domain Rearrangement of Protein Disulfide Isomerase Coupled with Exposure of Its Substrate-Binding Hydrophobic Surface. Serve, O., Kamiya, Y., Maeno, A. et al. J Mol Biol (2009). DOI 10.1016/j.jmb.2009.11.049 · PubMed

Other PDB entries of the same protein (UniProt P55059 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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