› 3tjn

X-ray diffraction
3Å resolution

HtrA1 catalytic domain, apo form

Released:
DOI: 10.2210/pdb3tjn/pdb
PDB entry 3tjn coloured by chain, front view.
PDB entry 3tjn coloured by chain, side view.
PDB entry 3tjn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional analysis of HtrA1 and its subdomains.
Eigenbrot C, Ultsch M, Lipari MT, Moran P, Lin SJ, Ganesan R, Quan C, Tom J, Sandoval W, van Lookeren Campagne M, Kirchhofer D
Structure 20 1040-50 (2012)
PMID: 22578544

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 Chains: A, B, D
Molecule details ›
Chains: A, B, D
Length: 228 amino acids
Theoretical weight: 24.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q92743 (Residues: 161-367; Coverage: 45%)
Gene names: HTRA, HTRA1, PRSS11
Sequence domains: Trypsin-like peptidase domain
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 ID29
Spacegroup: P6322
Unit cell:
a: 108.495Å b: 108.495Å c: 234.435Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.242 0.294
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

Features of cerebral autosomal recessive arteriopathy with subcortical infarcts and leukoencephalopathy.
Nozaki et al. (2014)
8 more

2 mentions without citation

NBCZone: Universal three-dimensional construction of eleven amino acids near the catalytic nucleophile and base in the superfamily of (chymo)trypsin-like serine fold proteases.
Denesyuk et al. (2020)
1 more