Structure analysis

crystal structure of human ERp44

X-ray diffraction
2.6Å resolution
Source organism: Homo sapiens
Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 17786.55 Å2
Buried surface area: 571.16 Å2
Dissociation area: 38.44 Å2
Dissociation energy (ΔGdiss): 0.78 kcal/mol
Dissociation entropy (TΔSdiss): -1.4 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-189699
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 33810.76 Å2
Buried surface area: 2911.92 Å2
Dissociation area: 885.19 Å2
Dissociation energy (ΔGdiss): -1.1 kcal/mol
Dissociation entropy (TΔSdiss): 13.95 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-189700

Macromolecules

Chain: A
Length: 382 amino acids
Theoretical weight: 44.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BS26 (Residues: 30-406; Coverage: 100%)
Gene names: ERP44, KIAA0573, TXNDC4, UNQ532/PRO1075
Pfam:
InterPro:
CATH: Glutaredoxin

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