2z9i

X-ray diffraction
2Å resolution

Crystal structure of RV0983 from Mycobacterium tuberculosis- Proteolytically active form

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero nonamer (preferred)
PDBe Complex ID:
PDB-CPX-129478 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Serine protease PepD Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 324 amino acids
Theoretical weight: 32.37 KDa
Source organism: Mycobacterium tuberculosis
UniProt:
  • Canonical: O53896 (Residues: 149-464; Coverage: 68%)
Gene names: Rv0983, htrA2, pepD
Sequence domains:
Structure domains:
SVEQV Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 5 amino acids
Theoretical weight: 561 Da
Source organism: Mycobacterium tuberculosis
GATV Chains: G, H, I
Molecule details ›
Chains: G, H, I
Length: 4 amino acids
Theoretical weight: 346 Da
Source organism: Mycobacterium tuberculosis

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: C2
Unit cell:
a: 149.584Å b: 89.067Å c: 69.408Å
α: 90° β: 97.55° γ: 90°
R-values:
R R work R free
0.228 0.225 0.272