Structure analysis

Crystal structure of human CDK2 complexed with a thiazolidinone inhibitor

X-ray diffraction
2.4Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 23532.91 Å2
Buried surface area: 3958.52 Å2
Dissociation area: 1,592.94 Å2
Dissociation energy (ΔGdiss): 13.61 kcal/mol
Dissociation entropy (TΔSdiss): 13.16 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-148886
Complex Portal ID: CPX-2006
Assembly 2
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Multimeric state: hetero dimer
Accessible surface area: 23482.63 Å2
Buried surface area: 3931.81 Å2
Dissociation area: 1,586.13 Å2
Dissociation energy (ΔGdiss): 11.11 kcal/mol
Dissociation entropy (TΔSdiss): 13.15 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-148886
Complex Portal ID: CPX-2006

Macromolecules

Chains: A, C
Length: 298 amino acids
Theoretical weight: 34.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P24941 (Residues: 1-298; Coverage: 100%)
Gene names: CDK2, CDKN2
Pfam: Protein kinase domain
InterPro:
CATH:

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Chains: B, D
Length: 258 amino acids
Theoretical weight: 29.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P20248 (Residues: 175-432; Coverage: 60%)
Gene names: CCN1, CCNA, CCNA2
Pfam:
InterPro:
CATH: Cyclin-like
SCOP: Cyclin

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