Structure analysis

Structure of the Predominant protein arginine methyltransferase PRMT1

X-ray diffraction
2.35Å resolution
Source organism: Rattus norvegicus
Assemblies composition:
hetero pentamer (preferred)
homo dimer
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero pentamer
Accessible surface area: 14707.07 Å2
Buried surface area: 746.33 Å2
Dissociation area: 162.18 Å2
Dissociation energy (ΔGdiss): -6.1 kcal/mol
Dissociation entropy (TΔSdiss): 0.72 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-162354
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 26148.04 Å2
Buried surface area: 4758.77 Å2
Dissociation area: 1,633.05 Å2
Dissociation energy (ΔGdiss): 21.4 kcal/mol
Dissociation entropy (TΔSdiss): 13.95 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-178989

Macromolecules

Chain: A
Length: 340 amino acids
Theoretical weight: 39.27 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q63009 (Residues: 14-353; Coverage: 96%)
Gene names: Hrmt1l2, Prmt1
Pfam: Methyltransferase domain
InterPro:
CATH:
SCOP: Arginine methyltransferase

Search similar proteins

Chains: B, C, D, E
Length: 19 amino acids
Theoretical weight: 1.67 KDa
Source organism: Rattus norvegicus
Expression system: Not provided

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