Structure analysis

Crystal structure of ribosomal protein L11 methyltransferase from Thermus thermophilus in complex with S-adenosyl-L-methionine

X-ray diffraction
2.3Å resolution
Source organism: Thermus thermophilus
Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 12695.21 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-183019
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 22967.27 Å2
Buried surface area: 2427.16 Å2
Dissociation area: 1,213.58 Å2
Dissociation energy (ΔGdiss): 9.24 kcal/mol
Dissociation entropy (TΔSdiss): 13.65 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-183020

Macromolecules

Chain: A
Length: 254 amino acids
Theoretical weight: 27.66 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q84BQ9 (Residues: 1-254; Coverage: 100%)
Gene names: TTHA0656, prmA
Pfam: Ribosomal protein L11 methyltransferase (PrmA)
InterPro:
CATH:

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