2B8H
A/NWS/whale/Maine/1/84 (H1N9) reassortant influenza virus neuraminidase
Summary for 2B8H
| Entry DOI | 10.2210/pdb2b8h/pdb |
| Related | 1a14 1nmb 1nmc 7nn9 |
| Descriptor | Neuraminidase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total) |
| Functional Keywords | 6-bladed beta-propeller, hydrolase |
| Biological source | Influenza A virus |
| Cellular location | Virion membrane (By similarity): P05803 |
| Total number of polymer chains | 4 |
| Total formula weight | 186692.07 |
| Authors | Smith, B.J.,Platis, D.,Cox, M.M.J.,Huyton, T.,Joosten, R.P.,McKimm-Breschkin, J.L.,Zhang, J.-G.,Luo, C.S.,Lou, M.-Z.,Garrett, T.P.J.,Labrou, N.E. (deposition date: 2005-10-07, release date: 2006-09-05, Last modification date: 2024-10-16) |
| Primary citation | Smith, B.J.,Huyton, T.,Joosten, R.P.,McKimm-Breschkin, J.L.,Zhang, J.G.,Luo, C.S.,Lou, M.Z.,Labrou, N.E.,Garrett, T.P. Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding. Acta Crystallogr.,Sect.D, 62:947-952, 2006 Cited by PubMed Abstract: The X-ray structure of influenza virus neuraminidase (NA) isolated from whale, subtype N9, has been determined at 2.2 A resolution and contains a tetrameric protein in the asymmetric unit. In structures of NA determined previously, a calcium ion is observed to coordinate amino acids near the substrate-binding site. In three of the NA monomers determined here this calcium is absent, resulting in structural alterations near the substrate-binding site. These changes affect the conformation of residues that participate in several key interactions between the enzyme and substrate and provide at a molecular level the basis of the structural and functional role of calcium in substrate and inhibitor binding. Several sulfate ions were identified in complex with the protein. These are located in the active site, occupying the space reserved for the substrate (sialic acid) carboxylate, and in positions leading away from the substrate-binding site. These sites offer a new opportunity for the design of inhibitors of influenza virus NA. PubMed: 16929094DOI: 10.1107/S0907444906020063 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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