Structure analysis

EarP bound with dTDP-rhamnose (soaked)

X-ray diffraction
2Å resolution
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: 30274.53 Å2
Buried surface area: 6754.2 Å2
Dissociation area: 955.33 Å2
Dissociation energy (ΔGdiss): 5.19 kcal/mol
Dissociation entropy (TΔSdiss): 14.06 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-123024

Macromolecules

Chains: A, B
Length: 382 amino acids
Theoretical weight: 44.22 KDa
Source organism: Neisseria meningitidis H44/76
Expression system: Escherichia coli
UniProt:
  • Canonical: E6MVV9 (Residues: 1-382; Coverage: 100%)
Gene names: NMH_0797, earP
Pfam: Elongation-Factor P (EF-P) rhamnosyltransferase EarP
InterPro: Protein-arginine rhamnosyltransferase EarP

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