6ieo

X-ray diffraction
1.83Å resolution

Crystal structure of Mycobacterium tuberculosis HtrA1 (Rv1223) in regulated conformation

Released:

Function and Biology Details

Reaction catalysed:
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable serine protease HtrA1 Chain: A
Molecule details ›
Chain: A
Length: 314 amino acids
Theoretical weight: 32.52 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: O06291 (Residues: 223-528; Coverage: 58%)
Gene names: Rv1223, degP, htrA, htrA1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: R3
Unit cell:
a: 107.114Å b: 107.114Å c: 61.529Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.191 0.227
Expression system: Escherichia coli