› 7jrx

X-ray diffraction
1.77Å resolution

Crystal structure of the R64F mutant of Bauhinia Bauhinioides complexed with Bovine Chymotrypsin

Released:
DOI: 10.2210/pdb7jrx/pdb
PDB entry 7jrx coloured by chain, front view.
PDB entry 7jrx coloured by chain, side view.
PDB entry 7jrx coloured by chain, top view.
Source organisms:
Primary publication:
Structural studies of complexes of kallikrein 4 with wild-type and mutated forms of the Kunitz-type inhibitor BbKI.
Li M, Srp J, Mareš M, Wlodawer A, Gustchina A
Acta Crystallogr D Struct Biol 77 1084-1098 (2021)
PMID: 34342281

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133409 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Chymotrypsin A chain A Chains: A, a
Molecule details ›
Chains: A, a
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-13; Coverage: 5%)
Chymotrypsin A chain B Chains: B, b
Molecule details ›
Chains: B, b
Length: 131 amino acids
Theoretical weight: 13.93 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 16-146; Coverage: 54%)
Sequence domains: Trypsin
Chymotrypsin A chain C Chains: C, c
Molecule details ›
Chains: C, c
Length: 97 amino acids
Theoretical weight: 10.07 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 149-245; Coverage: 40%)
Sequence domains: Trypsin
Kunitz-type serine protease inhibitor BbKI Chains: I, i
Molecule details ›
Chains: I, i
Length: 166 amino acids
Theoretical weight: 18.13 KDa
Source organism: Bauhinia bauhinioides
Expression system: Escherichia coli
UniProt:
  • Canonical: P83052 (Residues: 1-164; Coverage: 100%)
Sequence domains: Trypsin and protease inhibitor

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2221
Unit cell:
a: 60.018Å b: 60.693Å c: 425.535Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.208
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Between Protein Fold and Nucleophile Identity: Multiscale Modeling of the TEV Protease Enzyme-Substrate Complex.
Zlobin et al. (2022)

1 mention without citation

Structural studies of complexes of kallikrein 4 with wild-type and mutated forms of the Kunitz-type inhibitor BbKI.
Li et al. (2021)