› 5fxl

X-ray diffraction
1.78Å resolution

Structure of trypsin solved by MR from data collected by Direct Data Collection (DDC) using the ESRF RoboDiff goniometer

Released:
DOI: 10.2210/pdb5fxl/pdb
PDB entry 5fxl coloured by chain, front view.
PDB entry 5fxl coloured by chain, side view.
PDB entry 5fxl coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
RoboDiff: combining a sample changer and goniometer for highly automated macromolecular crystallography experiments.
Nurizzo D, Bowler MW, Caserotto H, Dobias F, Giraud T, Surr J, Guichard N, Papp G, Guijarro M, Mueller-Dieckmann C, Flot D, McSweeney S, Cipriani F, Theveneau P, Leonard GA
Acta Crystallogr D Struct Biol 72 966-75 (2016)
PMID: 27487827

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
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: 246 amino acids
Theoretical weight: 25.81 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 1-246; Coverage: 100%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand BEN 1 x BEN
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P212121
Unit cell:
a: 60.835Å b: 64.682Å c: 69.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.21

Quick links

Citations

13 citation in other articles

BRET-based RAS biosensors that show a novel small molecule is an inhibitor of RAS-effector protein-protein interactions.
Bery et al. (2018)
12 more

2 mentions without citation

RoboDiff: combining a sample changer and goniometer for highly automated macromolecular crystallography experiments.
Nurizzo et al. (2016)
1 more