3l8a

X-ray diffraction
1.54Å resolution

Crystal structure of MetC from Streptococcus mutans

Released:
Source organism: Streptococcus mutans UA159
Entry authors: Wang XJ, Fu TM, Su XD

Function and Biology Details

Reaction catalysed:
(1a) an L-cysteine-S-conjugate = a thiol + 2-aminoporp-2-enoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-184184 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cysteine-S-conjugate beta-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 421 amino acids
Theoretical weight: 48 KDa
Source organism: Streptococcus mutans UA159
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8DST5 (Residues: 1-387; Coverage: 100%)
Gene names: SMU_1674, metC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 59.377Å b: 64.346Å c: 99.315Å
α: 90° β: 100.93° γ: 90°
R-values:
R R work R free
0.177 0.176 0.199
Expression system: Escherichia coli