Structure analysis

Structural and biochemical studies of human PCNA complexes provide the basis for association with CDK/cyclin and rationale for inhibitor design

X-ray diffraction
2.8Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero hexamer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero hexamer
Accessible surface area: 36700 Å2
Buried surface area: 9400 Å2
Dissociation area: 2,200 Å2
Dissociation energy (ΔGdiss): 2 kcal/mol
Dissociation entropy (TΔSdiss): 27 kcal/mol
Interface energy (ΔGint): -55 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: hetero hexamer
Accessible surface area: 37100 Å2
Buried surface area: 9300 Å2
Dissociation area: 2,100 Å2
Dissociation energy (ΔGdiss): 2 kcal/mol
Dissociation entropy (TΔSdiss): 27 kcal/mol
Interface energy (ΔGint): -60 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, C, E, G, I, K
Length: 261 amino acids
Theoretical weight: 28.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12004 (Residues: 1-261; Coverage: 100%)
Gene name: PCNA
Pfam:
InterPro:
CATH: Proliferating Cell Nuclear Antigen
SCOP: DNA polymerase processivity factor

Search similar proteins

Chains: B, D, F, H, J, L
Length: 16 amino acids
Theoretical weight: 1.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)

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