› 5xx5

X-ray diffraction
1.38Å resolution

A BPTI-[5,55] variant with C14GA38I mutations

Released:
DOI: 10.2210/pdb5xx5/pdb
PDB entry 5xx5 coloured by chain, front view.
PDB entry 5xx5 coloured by chain, side view.
PDB entry 5xx5 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Hydrophobic surface residues can stabilize a protein through improved water-protein interactions.
Islam MM, Kobayashi K, Kidokoro SI, Kuroda Y
FEBS J 286 4122-4134 (2019)
PMID: 31175706

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133749 (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: 6.41 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 AR-NE3A
Spacegroup: P21
Unit cell:
a: 25.189Å b: 41.306Å c: 53.94Å
α: 90° β: 99.35° γ: 90°
R-values:
R R work R free
0.18 0.178 0.217
Expression system: Escherichia coli

Quick links

Citations

15 citation in other articles

The Stability Landscape of de novo TIM Barrels Explored by a Modular Design Approach.
Romero-Romero et al. (2021)
14 more

1 mention without citation

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