› 4ri0

X-ray diffraction
3.27Å resolution

Serine Protease HtrA3, mutationally inactivated

Released:
DOI: 10.2210/pdb4ri0/pdb
PDB entry 4ri0 coloured by chain, front view.
PDB entry 4ri0 coloured by chain, side view.
PDB entry 4ri0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and Functional Analysis of Human HtrA3 Protease and Its Subdomains.
Glaza P, Osipiuk J, Wenta T, Zurawa-Janicka D, Jarzab M, Lesner A, Banecki B, Skorko-Glonek J, Joachimiak A, Lipinska B
PLoS One 10 e0131142 (2015)
PMID: 26110759

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-160670 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease HTRA3 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 332 amino acids
Theoretical weight: 36.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P83110 (Residues: 130-453; Coverage: 74%)
Gene names: HTRA3, PRSP
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P43212
Unit cell:
a: 118.981Å b: 118.981Å c: 167.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.233
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Surface loops of trypsin-like serine proteases as determinants of function.
Goettig et al. (2019)
3 more

5 mentions without citation

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