2VSK: Hendra virus attachment glycoprotein

Hendra virus attachment glycoprotein in complex with human cell surface receptor ephrinB2. Determined by X-ray diffraction at 3.3 Å resolution. Released 20 May 2008.

Method
X-ray diffraction
Resolution
3.3 Å
Organisms
Hendra virus, Homo sapiens
Chains
4
Atoms
8,443
Mol. weight
125.11 kDa
Released
20 May 2008

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

Secondary structure: helices and β-sheets

2VSK contains 17 α-helices and 112 β-strands across 4 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, 38 β-strands

ElementResiduesLengthSheet
β-strand201-20221
β-strand215-226122
β-strand228-237102
β-strand244-257142
β-strand263-27192
β-strand279-28793
β-strand290-29783
α-helix303-3053
α-helix307-3093
β-strand314-32073
β-strand332-33543
β-strand340-34124
β-strand347-35044
β-strand35413
β-strand356-35834
β-strand361-371114
α-helix372-3743
α-helix379-3813
α-helix393-3975
β-strand407-417114
β-strand426-43054
β-strand43115
α-helix4321
β-strand442-44766
β-strand450-45566
β-strand46317
β-strand465-47176
β-strand47515
β-strand476-47946
β-strand48617
β-strand50918
β-strand512-51549
β-strand520-52679
β-strand533110
β-strand535-54179
β-strand544-55079
β-strand557-558210
β-strand56118
β-strand563-56861
β-strand571-57661
β-strand580-581210
β-strand58812
β-strand593-59421
β-strand59611
α-helix597-5982
Chain B: 2 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand32111
β-strand36-37211
β-strand46112
β-strand50112
β-strand51-53313
β-strand60-65611
α-helix66-672
β-strand78114
β-strand79-81315
β-strand82-84313
α-helix86-916
β-strand93116
β-strand102-104315
β-strand111-116611
β-strand134-138513
β-strand143114
β-strand152116
β-strand162-166513
Chain C: 6 helices, 41 β-strands
ElementResiduesLengthSheet
β-strand201-202217
β-strand215-2261218
β-strand228-2371018
β-strand244-2551218
β-strand265-271718
β-strand279-287919
β-strand290-297819
α-helix303-3053
β-strand314-320719
β-strand332-335419
β-strand340-341220
β-strand347-350420
β-strand354119
β-strand356-357220
β-strand361-3711120
α-helix372-3743
α-helix379-3813
α-helix394-3974
β-strand407-4171120
β-strand426-430520
β-strand431121
α-helix4321
β-strand442-447622
β-strand450-455622
β-strand463123
β-strand465-468422
β-strand469-471324
β-strand475121
β-strand476-477224
β-strand486123
β-strand505125
β-strand509126
β-strand512-515427
β-strand520-526727
β-strand533128
β-strand535-541727
β-strand544-550727
β-strand557-558228
β-strand561126
β-strand563-568617
β-strand571-576617
β-strand579-581328
β-strand588118
β-strand589-590228
β-strand593-594217
β-strand596117
α-helix597-5982
Chain D: 2 helices, 17 β-strands
ElementResiduesLengthSheet
β-strand32129
β-strand36-37229
β-strand46130
β-strand50130
β-strand51-53331
β-strand60-65629
α-helix66-672
β-strand78132
β-strand79-81333
β-strand82-84331
α-helix86-916
β-strand93134
β-strand102-104333
β-strand111-116629
β-strand123125
β-strand134-138531
β-strand143132
β-strand152134
β-strand162-166531

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Hemagglutinin-neuraminidaseA, Cprotein416Hendra virusO89343 (AlphaFold model)
Ephrin-B2B, Dprotein138Homo sapiensP52799 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>2VSK_1 HEMAGGLUTININ-NEURAMINIDASE (chains A, C)
ICLQKTTSTILKPRLISYTLPINTREGVCITDPLLAVDNGFFAYSHLEKIGSCTRGIAKQ
RIIGVGEVLDRGDKVPSMFMTNVWTPPNPSTIHHCSSTYHEDFYYTLCAVSHVGDPILNS
TSWTESLSLIRLAVRPKSDSGDYNQKYIAITKVERGKYDKVMPYGPSGIKQGDTLYFPAV
GFLPRTEFQYNDSNCPIIHCKYSKAENCRLSMGVNSKSHYILRSGLLKYNLSLGGDIILQ
FIEIADNRLTIGSPSKIYNSLGQPVFYQASYSWDTMIKLGDVDTVDPLRVQWRNNSVISR
PGQSQCPRFNVCPEVCWEGTYNDAFLIDRLNWVSAGVYLNSNQTAENPVFAVFKDNEILY
QVPLAEDDTNAQKTITDCFLLENVIWCISLVEIYDTGDSVIRPKLFAVKIPAQCSE
Sequence of entity 2 (B, D), FASTA
>2VSK_2 EPHRIN-B2 (chains B, D)
IVLEPIYWNSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDKDQAD
RCTIKKENTPLLNCAKPDQDIKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLEGLDN
QEGGVCQTRAMKILMKVG

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 O89343 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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