X-ray diffraction
1.9Å resolution

The Crystal Structure of a Putative Cysteine Protease from Cytophaga hutchinsonii to 1.9A

Entry authors: Stein AJ, Bigelow L, Trevino D, Buck K, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Transglutaminase-like enzymes, putative cysteine protease Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 293 amino acids
Theoretical weight: 33.16 KDa
Source organism: Cytophaga hutchinsonii ATCC 33406
Expression system: Escherichia coli BL21(DE3)
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 90.716Å b: 115.24Å c: 131.262Å
α: 90° β: 90° γ: 90°
R R work R free
0.189 0.187 0.22
Expression system: Escherichia coli BL21(DE3)