Structure analysis

Crystal Structure of Selenomethionine PcoC, a Copper Resistance Protein from Escherichia coli

X-ray diffraction
1.55Å resolution
Source organism: Escherichia coli
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 11192.11 Å2
Buried surface area: 757.31 Å2
Dissociation area: 378.65 Å2
Dissociation energy (ΔGdiss): -7.73 kcal/mol
Dissociation entropy (TΔSdiss): 11.01 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-175245

Macromolecules

Chains: A, B
Length: 104 amino acids
Theoretical weight: 11.3 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47454 (Residues: 23-126; Coverage: 100%)
Gene name: pcoC
Pfam: CopC domain
InterPro:
CATH: Immunoglobulin-like
SCOP: Copper resistance protein C (CopC, PcoC)

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