Structure analysis

Crystal structure of Zinc binding protein ZinT at 1.49 Angstrom from E. coli

X-ray diffraction
1.493Å resolution
Source organism: Escherichia coli K-12
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 10500 Å2
Buried surface area: 750 Å2
Dissociation area: 50 Å2
Dissociation energy (ΔGdiss): 11 kcal/mol
Dissociation entropy (TΔSdiss): -1 kcal/mol
Interface energy (ΔGint): -139 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly

Macromolecules

Chains: A, B
Length: 193 amino acids
Theoretical weight: 22.37 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P76344 (Residues: 24-216; Coverage: 100%)
Gene names: JW1956, b1973, yodA, zinT
Pfam: ZinT (YodA) periplasmic lipocalin-like zinc-recruitment
InterPro:
CATH: Lipocalin

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