6P7Y: Attachment glycoprotein

Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein globular domain in complex with the receptor ephrin-B2. Determined by X-ray diffraction at 2.84 Å resolution. Released 25 Sept 2019.

Method
X-ray diffraction
Resolution
2.84 Å
Organisms
Cedar virus, Homo sapiens
Chains
4
Atoms
9,852
Mol. weight
140.07 kDa
Ligands
NAG
Released
25 Sept 2019

Explore 6P7Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6P7Y contains 25 α-helices and 92 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: 9 helices, 33 β-strands

ElementResiduesLengthSheet
β-strand201-20331
β-strand224-22631
β-strand238-248112
β-strand251-260102
α-helix265-2673
β-strand268-280132
β-strand286-295102
α-helix299-3013
β-strand302-31093
β-strand313-32083
α-helix326-3294
α-helix332-3343
β-strand336-34273
α-helix347-3482
β-strand349-35243
α-helix355-3573
β-strand359-36024
β-strand366-36944
β-strand37115
β-strand375-37734
β-strand380-389104
α-helix397-4004
α-helix412-4187
β-strand42114
β-strand429-440124
β-strand443-45194
β-strand45216
α-helix4531
β-strand463-46865
β-strand471-47665
β-strand486-49275
β-strand49616
β-strand497-50045
β-strand53011
β-strand532-53657
β-strand541-54777
β-strand55411
β-strand556-56167
β-strand566-57167
β-strand578-589121
β-strand592-602111
β-strand612-61761
Chain B: 5 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand2918
α-helix30-323
β-strand33-3428
α-helix431
β-strand48-5039
β-strand57-6268
β-strand76-78310
β-strand79-8139
α-helix83-886
β-strand90111
β-strand99-101310
β-strand108-11368
β-strand130-13569
α-helix142-1443
β-strand149111
α-helix151-1544
β-strand159-16469
Chain C: 8 helices, 33 β-strands
ElementResiduesLengthSheet
β-strand201-202212
β-strand224-226312
β-strand238-2481113
β-strand251-2601013
β-strand270-2801113
β-strand286-2951013
α-helix299-3013
β-strand302-310914
β-strand313-320814
α-helix326-3294
α-helix332-3343
β-strand336-342714
α-helix347-3482
β-strand349-352414
α-helix355-3573
β-strand359-360215
β-strand366-369415
β-strand371-373316
β-strand375-377315
β-strand380-3891015
α-helix397-4004
α-helix412-4187
β-strand421115
β-strand429-4401215
β-strand443-451915
β-strand452117
α-helix4531
β-strand463-468616
β-strand471-476616
β-strand486-492716
β-strand496117
β-strand497-500416
β-strand530112
β-strand533-536418
β-strand541-547718
β-strand554112
β-strand556-561618
β-strand566-571618
β-strand578-5891212
β-strand592-6021112
β-strand612-617612
Chain D: 3 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand29119
α-helix30-323
β-strand33-34219
β-strand48-50320
β-strand57-62619
β-strand75121
β-strand76-78322
β-strand79-81320
α-helix83-886
β-strand90123
β-strand99-101322
β-strand108-113619
β-strand130-135620
β-strand140121
β-strand149123
α-helix151-1544
β-strand160-164520

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Attachment glycoproteinA, Cprotein430Cedar virusJ7H333 (AlphaFold model)
Ephrin-B2B, Dprotein144Homo sapiensP52799 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>6P7Y_1 Attachment glycoprotein (chains A, C)
SAMYSTNAYAELAGPPKIFCKSVSKDPDFRLKQIDYVIPVQQDRSICMNNPLLDISDGFF
TYIHYEGINSCKKSDSFKVLLSHGEIVDRGDYRPSLYLLSSHYHPYSMQVINCVPVTCNQ
SSFVFCHISNNTKTLDNSDYSSDEYYITYFNGIDRPKTKKIPINNMTADNRYIHFTFSGG
GGVCLGEEFIIPVTTVINTDVFTHDYCESFNCSVQTGKSLKEICSESLRSPTNSSRYNLN
GIMIISQNNMTDFKIQLNGITYNKLSFGSPGRLSKTLGQVLYYQSSMSWDTYLKAGFVEK
WKPFTPNWMNNTVISRPNQGNCPRYHKCPEICYGGTYNDIAPLDLGKDMYVSVILDSDQL
AENPEITVFNSTTILYKERVSKDELNTRSTTTSCFLFLDEPWCISVLETNRFNGKSIRPE
IYSYKIPKYC
Sequence of entity 2 (B, D), FASTA
>6P7Y_2 Ephrin-B2 (chains B, D)
SIVLEPIYWQSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDKDQA
DRCTIKKENTPLLNCAKPDQDIKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLEGLD
NQEGGVCQTRAMKILMKVGQDASS

Ligands and cofactors

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

Primary citation

Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus. Laing, E.D., Navaratnarajah, C.K., Cheliout Da Silva, S. et al. Proc Natl Acad Sci U S A (2019) 116:20707-20715. DOI 10.1073/pnas.1911773116 · PubMed

Other PDB entries of the same protein (UniProt J7H333 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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