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STRUCTURE of FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN

X-ray diffraction
1.91Å resolution
PDB entry 4osy coloured by chain, front view.
PDB entry 4osy coloured by chain, side view.
PDB entry 4osy 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: Isoaspartyl peptidase/L-asparaginase
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Multimeric state: homo dimer
Accessible surface area: 21135.95 Å2
Buried surface area: 3577.15 Å2
Dissociation area: 1,788.57 Å2
Dissociation energy (ΔGdiss): 16.22 kcal/mol
Dissociation entropy (TΔSdiss): 13.48 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-181624

Macromolecules

Isoaspartyl peptidase/L-asparaginase
Chains: A, B
Length: 309 amino acids
Theoretical weight: 32.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7L266 (Residues: 1-308; Coverage: 100%)
Gene names: ALP, ASRGL1, CRASH
Pfam: Asparaginase
InterPro:
Isoaspartyl peptidase/L-asparaginase in PDB entry 4osy, assembly 1, front view.
Isoaspartyl peptidase/L-asparaginase in PDB entry 4osy, assembly 1, side view.
Isoaspartyl peptidase/L-asparaginase in PDB entry 4osy, assembly 1, top view.
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