› 3gyl

X-ray diffraction
1.3Å resolution

Structure of Prostasin at 1.3 Angstroms resolution in complex with a Calcium Ion.

Released:
DOI: 10.2210/pdb3gyl/pdb
PDB entry 3gyl coloured by chain, front view.
PDB entry 3gyl coloured by chain, side view.
PDB entry 3gyl 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: 261 amino acids
Theoretical weight: 28.23 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

2 bound ligands:
Ligand CA 1 x CA
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: 54.112Å b: 54.039Å c: 82.553Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.153 0.178
Expression system: Spodoptera frugiperda

Quick links

Citations

8 review citations

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

3 mentions without citation

Protein conformational plasticity and complex ligand-binding kinetics explored by atomistic simulations and Markov models.
Plattner et al. (2015)
2 more