2KP1: Protein disulfide-isomerase

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

Method
Solution NMR
Organism
Humicola insolens
Chains
1
Atoms
926
Mol. weight
13.12 kDa
Released
27 Oct 2009

Explore 2KP1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2KP1 contains 5 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: 5 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand10-1121
α-helix14-207
β-strand28-3361
α-helix40-423
α-helix44-5613
β-strand64-6961
β-strand84-8851
β-strand97-9931
α-helix105-1106
α-helix111-1155

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein disulfide-isomeraseAprotein121Humicola insolensP55059 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KP1_1 Protein disulfide-isomerase (chains A)
GPLGSEGPVTVVVAKNYNEIVLDDTKDVLIEFYAPWCGHCKALAPKYEELGALYAKSEFK
DRVVIAKVDATANDVPDEIQGFPTIKLYPAGAKGQPVTYSGSRTVEDLIKFIAENGKYKA
A

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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