Structure analysis

Crystal structure of C-terminal domain of precorrin-6Y C5,15-methyltransferase from Rhodobacter capsulatus

X-ray diffraction
2.7Å resolution
Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo tetramer
Accessible surface area: 27500.22 Å2
Buried surface area: 12144.88 Å2
Dissociation area: 2,349.23 Å2
Dissociation energy (ΔGdiss): 17.98 kcal/mol
Dissociation entropy (TΔSdiss): 13.88 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-112680
Assembly 2 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 15978.39 Å2
Buried surface area: 3845.1 Å2
Dissociation area: 1,526.76 Å2
Dissociation energy (ΔGdiss): 8.42 kcal/mol
Dissociation entropy (TΔSdiss): 12.67 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-112679

Macromolecules

Chains: A, B
Length: 204 amino acids
Theoretical weight: 22.02 KDa
Source organism: Rhodobacter capsulatus SB 1003
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D5AV04 (Residues: 214-396; Coverage: 46%)
Gene names: RCAP_rcc02042, cobL
InterPro:
CATH: Vaccinia Virus protein VP39

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