› 7jqo

X-ray diffraction
1.6Å resolution

Crystal structure of the R64D mutant of Bauhinia Bauhinioides Kallikrein Inhibitor complexed with Human Kallikrein 4

Released:
DOI: 10.2210/pdb7jqo/pdb
PDB entry 7jqo coloured by chain, front view.
PDB entry 7jqo coloured by chain, side view.
PDB entry 7jqo 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

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160667 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Kallikrein-4 Chain: E
Molecule details ›
Chain: E
Length: 223 amino acids
Theoretical weight: 23.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y5K2 (Residues: 31-253; Coverage: 98%)
Gene names: EMSP1, KLK4, PRSS17, PSTS
Sequence domains: Trypsin
Kunitz-type serine protease inhibitor BbKI Chain: I
Molecule details ›
Chain: I
Length: 166 amino acids
Theoretical weight: 18.1 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

4 bound ligands:
Ligand 2PE 3 x 2PE
Ligand CD 1 x CD
Ligand SO4 1 x SO4
Ligand CL 2 x CL
1 modified residue:
Ligand CSO 2 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3121
Unit cell:
a: 103.804Å b: 103.804Å c: 86.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.114 0.112 0.152
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)

2 mentions without citation

Structural Basis of the Main Proteases of Coronavirus Bound to Drug Candidate PF-07321332.
Li et al. (2022)
1 more