5xko

X-ray diffraction
1.89Å resolution

Crystal structure of native Msmeg3575 deaminase from Mycobacterium smegmatis

Released:
Primary publication:
Selective Deamination of Mutagens by a Mycobacterial Enzyme.
J Am Chem Soc 139 10762-10768 (2017)
PMID: 28708393

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-106374 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CMP/dCMP-type deaminase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 158 amino acids
Theoretical weight: 17.13 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli
UniProt:
  • Canonical: A0QY90 (Residues: 2-159; Coverage: 99%)
Gene name: MSMEG_3575
Sequence domains: Cytidine and deoxycytidylate deaminase zinc-binding region

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21212
Unit cell:
a: 63.262Å b: 108.335Å c: 53.261Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.141 0.138 0.178
Expression system: Escherichia coli