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Ligands
Code Name Style Show Link
CA Calcium ion
0LP 5-acetamido-2,6-anhydro-3,5-dideoxy-3-[(2e)-3-phenylprop-2-en-1-yl]-D-glycero-L-altro-non-2-enonic acid
Non-standard Residues
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Glycosylation
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Code : 4GB1   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Synthesis and Evaluation of Novel 3-C-alkylated-Neu5Ac2en Derivatives as Probes of Influenza Virus Sialidase 150-loop flexibility
Release Data : 2012-09-26
Compound :
mol_id molecule chains
1 Neuraminidase A
ec: 3.2.1.18
fragment: UNP residues 81-470
Source :
mol_id organism_scientific
1 Influenza A virus  (taxid:385580)
strain: A/Duck/Ukraine/1/63 (H3N8)
Authors : Kerry, P.S., Rudrawar, S., Rameix-Welti, M.-A., Maggioni, A., Dyason, J.C., Rose, F.J., van der Werf, S., Thomson, R.J., Naffakh, N., Russell, R.J.M., von Itzstein, M.
Keywords : Enzyme, Vial protein, Glycosylation, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.62 Å )
Citation :

Synthesis and evaluation of novel 3-C-alkylated-Neu5Ac2en derivatives as probes of influenza virus sialidase 150-loop flexibility.

Rudrawar, S.,Kerry, P.S.,Rameix-Welti, M.A.  et al.
(2012)  Org.Biomol.Chem.  10 : 8628 - 8639

PubMed: 22976385
DOI: 10.1039/c2ob25627d

Chain : A
UniProt : Q07599 (NRAM_I63A3)
Reaction: EC: Evidence:
Physiological Direction:
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. 3.2.1.18 HAMAP- Rule:MF_04071
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