Structure analysis

Crystal structure of the tylM1 N,N-dimethyltransferase in complex with SAH and TDP-Qui3NMe2

X-ray diffraction
1.6Å resolution
Source organism: Streptomyces fradiae
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 19222.09 Å2
Buried surface area: 1550.66 Å2
Dissociation area: 775.33 Å2
Dissociation energy (ΔGdiss): 5.14 kcal/mol
Dissociation entropy (TΔSdiss): 12.7 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-161176
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 19392.77 Å2
Buried surface area: 1571.93 Å2
Dissociation area: 785.97 Å2
Dissociation energy (ΔGdiss): 5.7 kcal/mol
Dissociation entropy (TΔSdiss): 12.71 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-161176

Macromolecules

Chains: A, B, C, D
Length: 263 amino acids
Theoretical weight: 28.54 KDa
Source organism: Streptomyces fradiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P95748 (Residues: 1-255; Coverage: 100%)
Gene names: tylM1, tylMI
Pfam: Methyltransferase domain
InterPro:
CATH:

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