› 3e1x

X-ray diffraction
1.7Å resolution

The Crystal Structure of Apo Prostasin at 1.7 Angstroms Resolution

Released:
DOI: 10.2210/pdb3e1x/pdb
PDB entry 3e1x coloured by chain, front view.
PDB entry 3e1x coloured by chain, side view.
PDB entry 3e1x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations.
Spraggon G, Hornsby M, Shipway A, Tully DC, Bursulaya B, Danahay H, Harris JL, Lesley SA
Protein Sci 18 1081-94 (2009)
PMID: 19388054

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172540 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostasin heavy chain Chain: B
Molecule details ›
Chain: B
Length: 271 amino acids
Theoretical weight: 29.61 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q16651 (Residues: 45-305; Coverage: 83%)
Gene name: PRSS8
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P212121
Unit cell:
a: 53.556Å b: 54.071Å c: 82.678Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.168 0.215
Expression system: Spodoptera frugiperda

Quick links

Citations

7 review citations

Membrane-anchored serine proteases in health and disease.
Antalis et al. (2011)
6 more

3 mentions without citation

Allostery in trypsin-like proteases suggests new therapeutic strategies.
Gohara et al. (2011)
2 more