Structure analysis

Crystal structure of primase iron-sulfur domain (266-457)

X-ray diffraction
2.013Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: homo dimer
Accessible surface area: 17745.17 Å2
Buried surface area: 3592.34 Å2
Dissociation area: 920.41 Å2
Dissociation energy (ΔGdiss): 7.51 kcal/mol
Dissociation entropy (TΔSdiss): 11.98 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-155976
Assembly 2
Download    3D Visualisation
Multimeric state: homo dimer
Accessible surface area: 17421.58 Å2
Buried surface area: 3920.78 Å2
Dissociation area: 1,069.5 Å2
Dissociation energy (ΔGdiss): 19.39 kcal/mol
Dissociation entropy (TΔSdiss): 11.85 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-155976

Macromolecules

Chains: A, B
Length: 192 amino acids
Theoretical weight: 22.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49643 (Residues: 266-457; Coverage: 38%)
Gene names: PRIM2, PRIM2A
Pfam: Eukaryotic and archaeal DNA primase, large subunit
InterPro:

Search similar proteins