2VSM: Nipah virus attachment glycoprotein

Nipah virus attachment glycoprotein in complex with human cell surface receptor ephrinB2. Determined by X-ray diffraction at 1.8 Å resolution. Released 20 May 2008.

Method
X-ray diffraction
Resolution
1.8 Å
Organisms
Nipah virus, Homo sapiens
Chains
2
Atoms
5,272
Mol. weight
63.83 kDa
Ligands
NAG, IPA
Released
20 May 2008

Explore 2VSM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2VSM contains 14 α-helices and 48 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 7 helices, 32 β-strands

ElementResiduesLengthSheet
β-strand201-20331
β-strand215-225112
β-strand228-237102
β-strand244-257142
β-strand263-27192
β-strand279-28793
β-strand290-29783
β-strand314-32073
α-helix328-3314
β-strand332-33653
β-strand340-34124
β-strand347-35044
β-strand35413
β-strand356-35834
β-strand361-371114
α-helix372-3743
α-helix379-3813
α-helix394-3974
β-strand407-417114
α-helix418-4203
β-strand426-43054
β-strand43115
α-helix4321
β-strand442-44766
β-strand450-45566
β-strand465-47176
β-strand47515
β-strand476-47946
β-strand50911
β-strand511-51557
β-strand520-52677
β-strand53311
β-strand535-54177
β-strand544-55077
β-strand557-568121
β-strand571-581111
β-strand587-58822
β-strand591-59661
α-helix597-5982
Chain B: 7 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand3218
α-helix33-353
β-strand36-3728
β-strand4619
β-strand5019
β-strand51-53310
α-helix55-562
β-strand60-6568
α-helix66-683
α-helix75-773
β-strand78111
β-strand79-81312
β-strand82-84310
α-helix86-916
β-strand93113
β-strand102-104312
β-strand111-11668
β-strand133-138610
β-strand143111
α-helix145-1473
β-strand152113
α-helix154-1585
β-strand162-167610

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Hemagglutinin-neuraminidaseAprotein416Nipah virusQ9IH62 (AlphaFold model)
Ephrin-B2Bprotein140Homo sapiensP52799 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2VSM_1 HEMAGGLUTININ-NEURAMINIDASE (chains A)
ICLQKTSNQILKPKLISYTLPVVGQSGTCITDPLLAMDEGYFAYSHLERIGSCSRGVSKQ
RIIGVGEVLDRGDEVPSLFMTNVWTPPNPNTVYHCSAVYNNEFYYVLCAVSTVGDPILNS
TYWSGSLMMTRLAVKPKSNGGGYNQHQLALRSIEKGRYDKVMPYGPSGIKQGDTLYFPAV
GFLVRTEFKYNDSNCPITKCQYSKPENCRLSMGIRPNSHYILRSGLLKYNLSDGENPKVV
FIEISDQRLSIGSPSKIYDSLGQPVFYQASFSWDTMIKFGDVLTVNPLVVNWRNNTVISR
PGQSQCPRFNTCPEICWEGVYNDAFLIDRINWISAGVFLDSNQTAENPVFTVFKDNEILY
RAQLASEDTNAQKTITNCFLLKNKIWCISLVEIYDTGDNVIRPKLFAVKIPEQCTH
Sequence of entity 2 (B), FASTA
>2VSM_2 EPHRIN-B2 (chains B)
IVLEPIYWNSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDKDQAD
RCTIKKENTPLLNCAKPDQDIKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLEGLDN
QEGGVCQTRAMKILMKVGHH

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O64
IPAIsopropyl alcoholC3 H8 O1

Primary citation

Structural Basis of Nipah and Hendra Virus Attachment to Their Cell-Surface Receptor Ephrin-B2. Bowden, T.A., Aricescu, A.R., Gilbert, R.J. et al. Nat Struct Mol Biol (2008) 15:567. DOI 10.1038/NSMB.1435 · PubMed

Other PDB entries of the same protein (UniProt Q9IH62 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 2VSM directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.