Brand  (β version)

PDB ID: 1A14

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Ligands
Code Name Style Show Link
CA Calcium ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
BMA Beta-D-mannopyranose
MAN Alpha-D-mannopyranose
NAG 2-acetamido-2-deoxy-beta-D-glucopyranose
Modification
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Structure summary

Code : 1A14   PDBj   RCSB PDB   PDBe
Header : COMPLEX (ANTIBODY/ANTIGEN)
Title : COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 5 RESIDUE LINKER AND INFLUENZA VIRUS NEURAMINIDASE
Release Data : 1998-05-13
Compound :
mol_id molecule chains
1 NEURAMINIDASE N
ec: 3.2.1.18
fragment: RESIDUES 82 - 468
mol_id molecule chains
2 NC10 FV (HEAVY CHAIN) H
fragment: VH DOMAIN OF ANTI-NEURAMINIDASE ANTIBODY NC10 COVALENTLY JOINED BY A FIVE-RESIDUE POLYPEPTIDE LINKER
mol_id molecule chains
3 NC10 FV (LIGHT CHAIN) L
fragment: VL DOMAIN OF ANTI-NEURAMINIDASE ANTIBODY NC10 COVALENTLY JOINED BY A FIVE-RESIDUE POLYPEPTIDE LINKER
Source :
mol_id organism_scientific
1 Influenza A virus  (taxid:11320)
strain: N9, A/TERN/AUSTRALIA/G70C/75
mol_id organism_scientific organism_common expression_system
2 Mus musculus  (taxid:10090) House mouse Escherichia coli  (taxid:562)
mol_id organism_scientific organism_common expression_system
3 Mus musculus  (taxid:10090) House mouse Escherichia coli  (taxid:562)
Authors : Malby, R.L., Mccoy, A.J., Kortt, A.A., Hudson, P.J., Colman, P.M.
Keywords : COMPLEX (ANTIBODY-ANTIGEN), SINGLE-CHAIN ANTIBODY, GLYCOSYLATED PROTEIN, COMPLEX (ANTIBODY-ANTIGEN) complex
Exp. method : X-RAY DIFFRACTION ( 2.5 Å )
Citation :

Three-dimensional structures of single-chain Fv-neuraminidase complexes.

Malby, R.L.,McCoy, A.J.,Kortt, A.A.  et al.
(1998)  J.Mol.Biol.  279 : 901 - 910

PubMed: 9642070
DOI: 10.1006/jmbi.1998.1794

Recombinant Antineuraminidase Single Chain Antibody: Expression, Characterization, and Crystallization in Complex with Antigen

Malby, R.L.,Caldwell, J.B.,Gruen, L.C.  et al.
(1993)  Proteins  16 : 57

Reaction

Chain : N
UniProt : P03472 (NRAM_I75A5)
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, PubMed:23429702
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