› 3h6q

X-ray diffraction
1.64Å resolution

Macrocypin, a beta-trefoil cysteine protease inhibitor

Released:
DOI: 10.2210/pdb3h6q/pdb
PDB entry 3h6q coloured by chain, front view.
PDB entry 3h6q coloured by chain, side view.
PDB entry 3h6q coloured by chain, top view.
Source organism: Macrolepiota procera
Primary publication:
Versatile loops in mycocypins inhibit three protease families.
Renko M, Sabotic J, Mihelic M, Brzin J, Kos J, Turk D
J Biol Chem 285 308-16 (2010)
PMID: 19846555

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-110906 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macrocypin-1a Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 19.21 KDa
Source organism: Macrolepiota procera
Expression system: Escherichia coli
UniProt:
  • Canonical: B9V973 (Residues: 1-169; Coverage: 100%)
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P3121
Unit cell:
a: 77.11Å b: 77.11Å c: 60.92Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.162 0.193
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Cysteine cathepsins and extracellular matrix degradation.
Fonović et al. (2014)
7 more

4 mentions without citation

MAIN software for density averaging, model building, structure refinement and validation.
Turk D. (2013)
3 more