› 1coa

X-ray diffraction
2.2Å resolution

THE EFFECT OF CAVITY CREATING MUTATIONS IN THE HYDROPHOBIC CORE OF CHYMOTRYPSIN INHIBITOR 2

Released:
DOI: 10.2210/pdb1coa/pdb
PDB entry 1coa coloured by chain, front view.
PDB entry 1coa coloured by chain, side view.
PDB entry 1coa coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2.
Jackson SE, Moracci M, elMasry N, Johnson CM, Fersht AR
Biochemistry 32 11259-69 (1993)
PMID: 8218191

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133915 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin-chymotrypsin inhibitor-2A Chain: I
Molecule details ›
Chain: I
Length: 64 amino acids
Theoretical weight: 7.3 KDa
Source organism: Hordeum vulgare
Expression system: Not provided
UniProt:
  • Canonical: P01053 (Residues: 21-84; Coverage: 76%)
Sequence domains: Potato inhibitor I family
Structure domains: Trypsin Inhibitor V, subunit A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P622
Unit cell:
a: 68.925Å b: 68.925Å c: 53.094Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Hydrophobic core packing and protein design.
Lazar et al. (1998)
1 more

17 mentions without citation

MD Simulations of tRNA and Aminoacyl-tRNA Synthetases: Dynamics, Folding, Binding, and Allostery.
Li et al. (2015)
16 more