5XX2: A BPTI-[5,55] variant with C14GA38L mutations

A BPTI-[5,55] variant with C14GA38L mutations. Determined by X-ray diffraction at 1.12 Å resolution. Released 4 Jul 2018.

Method
X-ray diffraction
Resolution
1.12 Å
Organism
Bos taurus
Chains
2
Atoms
1,315
Mol. weight
13.4 kDa
Released
4 Jul 2018

Explore 5XX2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5XX2 contains 6 α-helices and 6 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.

Chains A and B: 3 helices, 3 β-strands

ElementResiduesLengthSheet
α-helix3-64
α-helix8-92
β-strand18-2471
β-strand29-3571
β-strand4511
α-helix48-558

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Pancreatic trypsin inhibitorA, Bprotein58Bos taurusP00974 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5XX2_1 Pancreatic trypsin inhibitor (chains A, B)
RPDFCLEPPYTGPGKARIIRYFYNAKAGLAQTFVYGGLRAKRNNFKSAEDALRTCGGA

Primary citation

Hydrophobic surface residues can stabilize a protein through improved water-protein interactions. Islam, M.M., Kobayashi, K., Kidokoro, S.I. et al. FEBS J (2019). DOI 10.1111/febs.14941 · PubMed

Other PDB entries of the same protein (UniProt P00974 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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