› 3e0n

X-ray diffraction
1.7Å resolution

The X-ray structure of Human Prostasin in complex with DFFR-chloromethyl ketone inhibitor

Released:
DOI: 10.2210/pdb3e0n/pdb
PDB entry 3e0n coloured by chain, front view.
PDB entry 3e0n coloured by chain, side view.
PDB entry 3e0n coloured by chain, top view.
Source organisms:
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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163499 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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: 45-309; Coverage: 84%)
Gene name: PRSS8
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
DPN-PHE-ARM Chain: A
Molecule details ›
Chain: A
Length: 3 amino acids
Theoretical weight: 467 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand GOL 3 x GOL
2 modified residues:
Ligand DPN 1 x DPN
Ligand ARM 1 x ARM

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P212121
Unit cell:
a: 37.677Å b: 75.88Å c: 79.179Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.157 0.202
Expression systems:
  • Spodoptera frugiperda
  • Not provided

Quick links

Citations

8 review citations

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