2R29: Envelope protein E

Neutralization of dengue virus by a serotype cross-reactive antibody elucidated by cryoelectron microscopy and x-ray crystallography. Determined by X-ray diffraction at 3.0 Å resolution. Released 25 Dec 2007.

Method
X-ray diffraction
Resolution
3.0 Å
Organisms
Dengue virus 2 Thailand/16681/84, Mus musculus
Chains
3
Atoms
4,234
Mol. weight
57.97 kDa
Released
25 Dec 2007

Explore 2R29 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2R29 contains 9 α-helices and 61 β-strands across 3 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: 2 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand30111
α-helix3021
β-strand305-314102
β-strand320-32782
β-strand33411
β-strand33713
β-strand34014
β-strand350-35122
α-helix3641
β-strand365-36622
β-strand369-37022
β-strand37714
β-strand38013
β-strand38713
β-strand39014
Chain H: 3 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand11-1225
β-strand18-2366
β-strand34-3967
β-strand46-5167
β-strand59-6027
α-helix62-643
β-strand7016
β-strand7316
β-strand78-8366
β-strand92-9547
β-strand110-11237
β-strand113-11425
α-helix118-1192
β-strand124-12748
β-strand14119
β-strand142-14878
β-strand154-156310
β-strand16619
β-strand16918
β-strand178-18148
β-strand18419
β-strand197-202610
α-helix203-2053
β-strand207-212610
Chain L: 4 helices, 27 β-strands
ElementResiduesLengthSheet
β-strand6111
β-strand12-13212
β-strand19-21313
β-strand23111
β-strand30114
β-strand35114
β-strand37-42615
β-strand50115
β-strand52116
α-helix571
β-strand58116
α-helix591
β-strand67-70413
β-strand75-79513
β-strand89-94615
β-strand102115
β-strand106-107215
β-strand109-110212
α-helix114-1152
β-strand122117
α-helix123-1253
β-strand133118
β-strand136-137217
β-strand143119
β-strand151120
β-strand163-167517
β-strand177119
β-strand179-183517
β-strand186118
β-strand195-200620
β-strand205-210620

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Envelope protein EAprotein97Dengue virus 2 Thailand/16681/84P29991
Heavy chain of Fab 1A1D-2Hprotein216Mus musculusP01863 (AlphaFold model)
Light chain of Fab 1A1D-2Lprotein217Mus musculusP01660 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2R29_1 Envelope protein E (chains A)
SYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPI
VTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKK
Sequence of entity 2 (H), FASTA
>2R29_2 Heavy chain of Fab 1A1D-2 (chains H)
EVQLQQSGAELVKPGASVKLSCTASGFNIKDTYMHWVKQRPEQGLEWIGRIDPANGYSKY
DPKFQGKATITADTSSNAAYLQLSSLTSEDTAVYFCARDYEGFAYWGQGTLVTVSSAKTT
PPSVYPLAPGAAAATSSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTL
SSSVTVTSSTWPSQTITCNVAHPASSTKVDKKIEPR
Sequence of entity 3 (L), FASTA
>2R29_3 Light chain of Fab 1A1D-2 (chains L)
DIVLTQSPASLAVSLGQRATISCRASESVVRYGNSFMHWYQQKPGQPPKLLIYRASSLES
GIPTRFSGSGSRTDFTLTINPVEADDVATYYCQQTNVDPWAFGGGTKLEIKRADAAPTVS
IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMS
STLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNE

Primary citation

Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins. Lok, S.M., Kostyuchenko, V., Nybakken, G.E. et al. Nat Struct Mol Biol (2008) 15:312-317. DOI 10.1038/nsmb.1382 · PubMed

Other PDB entries of the same protein (UniProt P29991), best resolution first:

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