› 7a54

X-ray diffraction
2.7Å resolution

Two copies of the catalytic domain of NanA sialidase from Streptococcus pneumoniae juxtaposed in the P212121 space group, in complex with DANA

Released:
DOI: 10.2210/pdb7a54/pdb
PDB entry 7a54 coloured by chain, front view.
PDB entry 7a54 coloured by chain, side view.
PDB entry 7a54 coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Polyvalent Transition-State Analogues of Sialyl Substrates Strongly Inhibit Bacterial Sialidases*.
Assailly C, Bridot C, Saumonneau A, Lottin P, Roubinet B, Krammer EM, François F, Vena F, Landemarre L, Alvarez Dorta D, Deniaud D, Grandjean C, Tellier C, Pascual S, Montembault V, Fontaine L, Daligault F, Bouckaert J, Gouin SG
Chemistry 27 3142-3150 (2021)
PMID: 33150981

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-548983 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 498 amino acids
Theoretical weight: 56.14 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P62575 (Residues: 318-791; Coverage: 48%)
Gene name: nanA
Sequence domains: BNR repeat-like domain

Ligands and Environments

1 bound ligand:
Ligand DAN 2 x DAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 51.87Å b: 96.194Å c: 220.602Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.247
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Sialidase Inhibitors with Different Mechanisms.
Keil et al. (2022)
3 other articles

1 mention without citation

Hold your horses: The receptor-binding domains of SARS-CoV-2, SARS-CoV, and hCoV-NL63 bind equine ACE2.
Nawrath et al. (2022)