3nzi

X-ray diffraction
2.75Å resolution

Substrate induced remodeling of the active site regulates HtrA1 activity

Released:

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-187741 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease HTRA1 Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 36.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92743 (Residues: 158-480; Coverage: 71%)
Gene names: HTRA, HTRA1, PRSS11
Sequence domains:
Structure domains: Trypsin-like serine proteases
Citrate synthase, mitochondrial Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 850 Da
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: Q9CZU6 (Residues: 371-377; Coverage: 2%)
Gene name: Cs

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: R3
Unit cell:
a: 105.965Å b: 105.965Å c: 118.336Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.2 0.249
Expression systems:
  • Escherichia coli
  • Not provided