› 4m4v

X-ray diffraction
1.84Å resolution

Structural evaluation R171L mutant of the aspergillus fumigatus kdnase (sialidase)

Released:
DOI: 10.2210/pdb4m4v/pdb
PDB entry 4m4v coloured by chain, front view.
PDB entry 4m4v coloured by chain, side view.
PDB entry 4m4v coloured by chain, top view.
Source organism: Aspergillus fumigatus Af293
Entry authors: Telford JC, Taylor GL

Function and Biology Details

Reaction catalysed: 
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175839 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exo-alpha-sialidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 422 amino acids
Theoretical weight: 46.23 KDa
Source organism: Aspergillus fumigatus Af293
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4WQS0 (Residues: 1-406; Coverage: 100%)
Gene name: AFUA_4G13800
Sequence domains: BNR repeat-like domain
Structure domains: Neuraminidase

Ligands and Environments

4 bound ligands:
Ligand DAN 1 x DAN
Ligand GOL 3 x GOL
Ligand NO3 4 x NO3
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 75.88Å b: 57.97Å c: 94.64Å
α: 90° β: 99.89° γ: 90°
R-values:
R R work R free
0.156 0.154 0.194
Expression system: Escherichia coli

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