6PD4: Hendra Virus Attachment G Glycoprotein

Crystal Structure of Hendra Virus Attachment G Glycoprotein. Determined by X-ray diffraction at 2.2 Å resolution. Released 27 Nov 2019.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Hendra henipavirus
Chains
2
Atoms
7,734
Mol. weight
104.01 kDa
Ligands
NAG
Released
27 Nov 2019

Explore 6PD4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6PD4 contains 15 α-helices and 67 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, 34 β-strands

ElementResiduesLengthSheet
β-strand178-18031
α-helix185-1873
β-strand201-20221
α-helix203-2042
β-strand20512
β-strand215-225112
β-strand228-237102
β-strand244-257142
β-strand263-27192
β-strand279-28793
β-strand290-29783
α-helix310-3123
β-strand314-32073
β-strand332-33763
β-strand339-34134
β-strand347-35044
β-strand35413
β-strand356-35834
β-strand361-371114
α-helix372-3743
α-helix379-3813
α-helix394-3974
β-strand407-417114
β-strand425-43064
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-strand53318
β-strand535-54177
β-strand544-55077
β-strand55718
β-strand558-568111
β-strand571-582121
β-strand587-596101
Chain B: 8 helices, 33 β-strands
ElementResiduesLengthSheet
β-strand178-18039
α-helix185-1873
β-strand201-20229
α-helix204-2063
β-strand215-2251110
β-strand228-2371010
α-helix2431
β-strand244-2571410
β-strand263-271910
β-strand279-287911
β-strand290-297811
α-helix310-3123
β-strand314-320711
β-strand332-337611
β-strand339-341312
β-strand347-350412
β-strand354111
β-strand356-358312
β-strand361-3711112
α-helix372-3743
α-helix379-3813
α-helix394-3974
β-strand407-4171112
β-strand425-430612
β-strand431113
α-helix4321
β-strand442-447614
β-strand450-455614
β-strand465-471714
β-strand475113
β-strand476-479414
β-strand50919
β-strand511-515515
β-strand520-526715
β-strand533116
β-strand535-541715
β-strand544-550715
β-strand557116
β-strand558-568119
β-strand571-582129
β-strand587-596109

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Attachment glycoproteinA, Bprotein441Hendra henipavirusO89343 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6PD4_1 Attachment glycoprotein (chains A, B)
YRPISQGVSDLVGLPNQICLQKTTSTILKPRLISYTLPINTREGVCITDPLLAVDNGFFA
YSHLEKIGSCTRGIAKQRIIGVGEVLDRGDKVPSMFMTNVWTPPNPSTIHHCSSTYHEDF
YYTLCAVSHVGDPILNSTSWTESLSLIRLAVRPKSDSGDYNQKYIAITKVERGKYDKVMP
YGPSGIKQGDTLYFPAVGFLPRTEFQYNDSNCPIIHCKYSKAENCRLSMGVNSKSHYILR
SGLLKYNLSLGGDIILQFIEIADNRLTIGSPSKIYNSLGQPVFYQASYSWDTMIKLGDVD
TVDPLRVQWRNNSVISRPGQSQCPRFNVCPEVCWEGTYNDAFLIDRLNWVSAGVYLNSNQ
TAENPVFAVFKDNEILYQVPLAEDDTNAQKTITDCFLLENVIWCISLVEIYDTGDSVIRP
KLFAVKIPAQCSESGRGLVPR

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O62

Water and common crystallization additives (SO4) are not listed.

Primary citation

New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2. Xu, K., Chan, Y.P., Rajashankar, K.R. et al. PLoS One (2012) 7:e48742. DOI 10.1371/journal.pone.0048742 · 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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