Structure analysis

CRYSTAL STRUCTURE OF E3 LIGASE ITCH WITH A UB VARIANT

X-ray diffraction
3.03Å resolution
Source organism: Homo sapiens
Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 21981.42 Å2
Buried surface area: 1462.93 Å2
Dissociation area: 731.46 Å2
Dissociation energy (ΔGdiss): -0.6 kcal/mol
Dissociation entropy (TΔSdiss): 10.77 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-143398
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 4719.97 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-143327

Macromolecules

Chain: A
Length: 394 amino acids
Theoretical weight: 47.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96J02 (Residues: 524-899; Coverage: 42%)
Gene name: ITCH
Pfam: HECT-domain (ubiquitin-transferase)
InterPro:

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Chains: B, C
Length: 84 amino acids
Theoretical weight: 9.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 533-607; Coverage: 11%)
Gene name: UBC
Pfam: Ubiquitin family
InterPro:

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