2zhx

X-ray diffraction
3.1Å resolution

Crystal structure of Uracil-DNA Glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor

Released:

Function and Biology Details

Reaction catalysed:
Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Uracil-DNA glycosylase Chains: A, C, E, G, I, K, M
Molecule details ›
Chains: A, C, E, G, I, K, M
Length: 238 amino acids
Theoretical weight: 25.81 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WFQ9 (Residues: 1-227; Coverage: 100%)
Gene names: MTCY349.11, Rv2976c, ung
Sequence domains: Uracil DNA glycosylase superfamily
Structure domains: Uracil-DNA glycosylase-like domain
Uracil-DNA glycosylase inhibitor Chains: B, D, F, H, J, L, N
Molecule details ›
Chains: B, D, F, H, J, L, N
Length: 84 amino acids
Theoretical weight: 9.48 KDa
Source organism: Bacillus phage PBS2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14739 (Residues: 1-84; Coverage: 100%)
Gene name: UGI
Sequence domains: Uracil-DNA glycosylase inhibitor
Structure domains: Bacteriophage PBS2, uracil-glycosylase inhibitor

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 201.143Å b: 64.274Å c: 203.677Å
α: 90° β: 109.72° γ: 90°
R-values:
R R work R free
0.236 0.234 0.276
Expression system: Escherichia coli BL21(DE3)