Structure analysis

Structure of the N-terminal four domains of the complement regulator Rat Crry

X-ray diffraction
2.5Å resolution
Source organism: Rattus norvegicus
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 16500 Å2
Buried surface area: 2800 Å2
Dissociation area: 100 Å2
Dissociation energy (ΔGdiss): -1 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Interface energy (ΔGint): -9 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 290 amino acids
Theoretical weight: 31.93 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q63135 (Residues: 1-288; Coverage: 48%)
Gene names: Cr1l, Crry
Pfam: Sushi repeat (SCR repeat)
InterPro:
CATH: Complement Module, domain 1

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