› 6b6o

X-ray diffraction
2.4Å resolution

Orthorhombic trypsin cryocooled to 100 K with 20% xylose as cryoprotectant

Released:
DOI: 10.2210/pdb6b6o/pdb
PDB entry 6b6o coloured by chain, front view.
PDB entry 6b6o coloured by chain, side view.
PDB entry 6b6o coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.
Juers DH, Farley CA, Saxby CP, Cotter RA, Cahn JKB, Holton-Burke RC, Harrison K, Wu Z
OpenAccess logo Acta Crystallogr D Struct Biol 74 922-938 (2018)
PMID: 30198901

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease 1 Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
Expression system: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

5 bound ligands:
Ligand CA 1 x CA
Ligand BEN 1 x BEN
Ligand SO4 2 x SO4
Ligand XYP 1 x XYP
Ligand XYS 1 x XYS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION NOVA
Spacegroup: P212121
Unit cell:
a: 54.439Å b: 58.172Å c: 65.943Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.24 0.345
Expression system: Bos taurus

Quick links

Citations

3 citation in other articles

The low-cost Shifter microscope stage transforms the speed and robustness of protein crystal harvesting.
Wright et al. (2021)
2 more

1 mention without citation

The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.
Juers et al. (2018)