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Rational design of a novel enzyme - efficient thioester hydrolysis enabled by the incorporation of a single His residue into human glutathione transferase A1-1

X-ray diffraction
2.07Å resolution
PDB entry 1usb coloured by chain, front view.
PDB entry 1usb coloured by chain, side view.
PDB entry 1usb coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Glutathione S-transferase A1
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Multimeric state: homo dimer
Accessible surface area: 20615.02 Å2
Buried surface area: 5185.99 Å2
Dissociation area: 1,651.82 Å2
Dissociation energy (ΔGdiss): 16.84 kcal/mol
Dissociation entropy (TΔSdiss): 13.23 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-140083

Macromolecules

Glutathione S-transferase A1
Chains: A, B
Length: 225 amino acids
Theoretical weight: 25.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08263 (Residues: 2-222; Coverage: 100%)
Gene name: GSTA1
Pfam:
InterPro:
CATH:
SCOP:
Glutathione S-transferase A1 in PDB entry 1usb, assembly 1, front view.
Glutathione S-transferase A1 in PDB entry 1usb, assembly 1, side view.
Glutathione S-transferase A1 in PDB entry 1usb, assembly 1, top view.
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