Structure analysis

HUMAN ASPARTYLGLUCOSAMINIDASE

X-ray diffraction
2Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero tetramer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero tetramer
Accessible surface area: 20904.88 Å2
Buried surface area: 17662.91 Å2
Dissociation area: 2,709.02 Å2
Dissociation energy (ΔGdiss): 30.36 kcal/mol
Dissociation entropy (TΔSdiss): 14 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-149092

Macromolecules

Chains: A, C
Length: 162 amino acids
Theoretical weight: 17.29 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P20933 (Residues: 24-185; Coverage: 50%)
Gene name: AGA
Pfam: Asparaginase
InterPro:
SCOP: (Glycosyl)asparaginase

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Chains: B, D
Length: 141 amino acids
Theoretical weight: 15.09 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P20933 (Residues: 206-346; Coverage: 44%)
Gene name: AGA
Pfam: Asparaginase
InterPro:
CATH: (Glycosyl)asparaginase
SCOP: (Glycosyl)asparaginase

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