Structure analysis

Crystal structure of hTEAD2 in complex with a trisubstituted pyrazole inhibitor

X-ray diffraction
2Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 10691.57 Å2
Buried surface area: 689.98 Å2
Dissociation area: 344.99 Å2
Dissociation energy (ΔGdiss): -7.53 kcal/mol
Dissociation entropy (TΔSdiss): 3.57 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-172328
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 11564.07 Å2
Buried surface area: 718.17 Å2
Dissociation area: 359.09 Å2
Dissociation energy (ΔGdiss): -6.39 kcal/mol
Dissociation entropy (TΔSdiss): 3.61 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-172328

Macromolecules

Chains: A, B
Length: 240 amino acids
Theoretical weight: 27.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15562 (Residues: 217-447; Coverage: 52%)
Gene names: TEAD2, TEF4
Pfam: YAP binding domain
InterPro: YAP binding domain

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