2gac

X-ray diffraction
2.1Å resolution

T152C MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM

Released:

Function and Biology Details

Reaction catalysed:
N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-D-glucosaminylamine + L-aspartate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-175278 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glycosylasparaginase alpha chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 151 amino acids
Theoretical weight: 16.82 KDa
Source organism: Elizabethkingia meningoseptica
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47898 (Residues: 46-196; Coverage: 51%)
Sequence domains: Asparaginase
Glycosylasparaginase beta chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 144 amino acids
Theoretical weight: 15.38 KDa
Source organism: Elizabethkingia meningoseptica
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47898 (Residues: 198-340; Coverage: 49%)
Sequence domains: Asparaginase
Structure domains: (Glycosyl)asparaginase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 46.2Å b: 97.3Å c: 61.8Å
α: 90° β: 90.3° γ: 90°
R-values:
R R work R free
0.233 0.233 0.28
Expression system: Escherichia coli