2ZVX: Pancreatic trypsin inhibitor

Structure of a BPTI-[5,55] variant containing Gly/Val at the 14/38th positions. Determined by X-ray diffraction at 1.09 Å resolution. Released 13 Oct 2009.

Method
X-ray diffraction
Resolution
1.09 Å
Organism
Bos taurus
Chains
2
Atoms
1,026
Mol. weight
13.08 kDa
Released
13 Oct 2009

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

Secondary structure: helices and β-sheets

2ZVX contains 5 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.

Chain A: 2 helices, 3 β-strands

ElementResiduesLengthSheet
α-helix8-92
β-strand18-2471
β-strand29-3571
β-strand4511
α-helix48-558
Chain B: 3 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix3-64
α-helix8-92
β-strand18-2472
β-strand29-3572
β-strand4512
α-helix48-558

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Pancreatic trypsin inhibitorA, Bprotein58Bos taurusP00974 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2ZVX_1 Pancreatic trypsin inhibitor (chains A, B)
RPDFCLEPPYTGPGKARIIRYFYNAKAGLAQTFVYGGVRAKRNNFKSAEDALRTCGGA

Primary citation

Thermodynamic and structural analysis of highly stabilized BPTIs by single and double mutations. Islam, M.M., Sohya, S., Noguchi, K. et al. Proteins (2009) 77:962-970. DOI 10.1002/prot.22522 · PubMed

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

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