Structure analysis

Crystal structure of the C-terminal PH domain of pleckstrin in complex with D-myo-Ins(1,2,3,4,5)P5

X-ray diffraction
1.75Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 5976.09 Å2
Buried surface area: 577.64 Å2
Dissociation area: 288.82 Å2
Dissociation energy (ΔGdiss): 11.93 kcal/mol
Dissociation entropy (TΔSdiss): 5.32 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140179
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 5977.4 Å2
Buried surface area: 575.83 Å2
Dissociation area: 287.91 Å2
Dissociation energy (ΔGdiss): 14.09 kcal/mol
Dissociation entropy (TΔSdiss): 5.32 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140179
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 6005.21 Å2
Buried surface area: 569.37 Å2
Dissociation area: 284.69 Å2
Dissociation energy (ΔGdiss): 12.63 kcal/mol
Dissociation entropy (TΔSdiss): 5.32 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140179

Macromolecules

Chains: A, B, C
Length: 109 amino acids
Theoretical weight: 12.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08567 (Residues: 244-347; Coverage: 30%)
Gene names: P47, PLEK
Pfam: PH domain
InterPro:
CATH: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
SCOP: Pleckstrin-homology domain (PH domain)

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