4chg

X-ray diffraction
2.1Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ribonuclease VapC15 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 133 amino acids
Theoretical weight: 15.01 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WF97 (Residues: 1-132; Coverage: 100%)
Gene names: MTCY39.07c, Rv2010, vapC15
Sequence domains: PIN domain
Structure domains: 5'-nuclease
Antitoxin VapB15 Chains: G, H, I, J
Molecule details ›
Chains: G, H, I, J
Length: 88 amino acids
Theoretical weight: 9.96 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WLM7 (Residues: 1-80; Coverage: 100%)
Gene names: MTCY39.08c, Rv2009, vapB15
Sequence domains: Bacterial antitoxin of type II TA system, VapB

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P212121
Unit cell:
a: 86.16Å b: 131.2Å c: 149.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.167 0.2
Expression system: Escherichia coli BL21(DE3)