› 2zvx

X-ray diffraction
1.09Å resolution

Structure of a BPTI-[5,55] variant containing Gly/Val at the 14/38th positions

Released:
DOI: 10.2210/pdb2zvx/pdb
PDB entry 2zvx coloured by chain, front view.
PDB entry 2zvx coloured by chain, side view.
PDB entry 2zvx coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Thermodynamic and structural analysis of highly stabilized BPTIs by single and double mutations.
Islam MM, Sohya S, Noguchi K, Kidokoro S, Yohda M, Kuroda Y
Proteins 77 962-70 (2009)
PMID: 19830687

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133762 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pancreatic trypsin inhibitor Chains: A, B
Molecule details ›
Chains: A, B
Length: 58 amino acids
Theoretical weight: 6.4 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 24.962Å b: 40.844Å c: 54.829Å
α: 90° β: 100.55° γ: 90°
R-values:
R R work R free
0.179 not available 0.212
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods.
Nowak et al. (2010)
6 more

1 mention without citation

Hydrophobic surface residues can stabilize a protein through improved water-protein interactions.
Islam et al. (2019)