› 3num

X-ray diffraction
2.75Å resolution

Substrate induced remodeling of the active site regulates HtrA1 activity

Released:
DOI: 10.2210/pdb3num/pdb
PDB entry 3num coloured by chain, front view.
PDB entry 3num coloured by chain, side view.
PDB entry 3num 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

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease HTRA1 Chain: A
Molecule details ›
Chain: A
Length: 332 amino acids
Theoretical weight: 36.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92743 (Residues: 157-480; Coverage: 71%)
Gene names: HTRA, HTRA1, PRSS11
Sequence domains:
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: R3
Unit cell:
a: 109.476Å b: 109.476Å c: 113.956Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.242 0.287
Expression system: Escherichia coli

Quick links

Citations

15 review citations

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

6 mentions without citation

Structural and Functional Analysis of Human HtrA3 Protease and Its Subdomains.
Glaza et al. (2015)
5 more