› 3nwu

X-ray diffraction
3.2Å resolution

Substrate induced remodeling of the active site regulates HtrA1 activity

Released:
DOI: 10.2210/pdb3nwu/pdb
PDB entry 3nwu coloured by chain, front view.
PDB entry 3nwu coloured by chain, side view.
PDB entry 3nwu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Substrate-induced remodeling of the active site regulates human HTRA1 activity.
Truebestein L, Tennstaedt A, Mönig T, Krojer T, Canellas F, Kaiser M, Clausen T, Ehrmann M
Nat Struct Mol Biol 18 386-8 (2011)
PMID: 21297635

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-187740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease HTRA1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 227 amino acids
Theoretical weight: 24.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92743 (Residues: 157-375; Coverage: 48%)
Gene names: HTRA, HTRA1, PRSS11
Sequence domains: Trypsin-like peptidase domain
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43212
Unit cell:
a: 153.671Å b: 153.671Å c: 89.835Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.209
Expression system: Escherichia coli

Quick links

Citations

15 review citations

HTRA proteases: regulated proteolysis in protein quality control.
Clausen et al. (2011)
14 more

4 mentions without citation

Multiple origins of viral capsid proteins from cellular ancestors.
Krupovic et al. (2017)
3 more