› 6ieo

X-ray diffraction
1.83Å resolution

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

Released:
DOI: 10.2210/pdb6ieo/pdb
PDB 6ieo coloured by chain and viewed from the front.
PDB 6ieo coloured by chain and viewed from the side.
PDB 6ieo coloured by chain and viewed from the top.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism.
Gupta AK, Behera D, Gopal B
Acta Crystallogr F Struct Biol Commun 74 803-809 (2018)
PMID: 30511675

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
Sequence domains:

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:
Ligand PMS 1 x PMS
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

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