6CDM: VFP7.04 heavy chain

Structure of vaccine-elicited HIV-1 neutralizing antibody vFP7.04 in complex with HIV-1 fusion peptide residue 512-519. Determined by X-ray diffraction at 2.41 Å resolution. Released 16 May 2018.

Method
X-ray diffraction
Resolution
2.41 Å
Organisms
Mus musculus, Human immunodeficiency virus 1
Chains
6
Atoms
7,075
Mol. weight
96.97 kDa
Released
16 May 2018

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

Secondary structure: helices and β-sheets

6CDM contains 38 α-helices and 94 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: 10 helices, 24 β-strands

ElementResiduesLengthSheet
β-strand3-641
α-helix71
β-strand10-1232
β-strand18-2581
α-helix29-313
β-strand33-4082
β-strand44-5182
β-strand57-5932
α-helix61-633
β-strand6411
β-strand67-7261
β-strand77-8261
α-helix84-863
β-strand88-9582
β-strand10312
β-strand107-11152
α-helix115-1162
β-strand11713
α-helix118-1192
β-strand120-12454
α-helix128-1303
β-strand131-13224
β-strand135-145114
β-strand14613
β-strand151-15445
α-helix155-1573
β-strand15915
β-strand163-16534
α-helix166-1683
β-strand169-17024
β-strand176-185104
β-strand194-20075
α-helix201-2033
β-strand205-21175
Chain B: 9 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand4-746
β-strand10-1457
β-strand19-2576
β-strand27C18
β-strand3118
β-strand33-3867
β-strand45-4957
β-strand53-5427
α-helix551
β-strand62-6766
β-strand70-7566
α-helix80-823
β-strand84-9077
α-helix961
β-strand97-9827
β-strand102-10767
β-strand11119
α-helix112-1132
β-strand114-118510
α-helix119-1213
α-helix122-1254
β-strand129-1391110
β-strand14019
β-strand145-150611
β-strand153-154211
α-helix1551
β-strand159-163510
α-helix164-1674
β-strand173-1821010
α-helix183-1864
β-strand191-197711
β-strand205-210611
Chain D: 10 helices, 24 β-strands
ElementResiduesLengthSheet
β-strand3-6412
α-helix7-93
β-strand10-12313
β-strand18-25812
α-helix29-313
β-strand33-40813
β-strand44-51813
β-strand57-59313
α-helix61-633
β-strand64112
β-strand67-72612
β-strand77-82612
α-helix84-863
β-strand88-95813
β-strand103113
β-strand107-111513
α-helix115-1162
β-strand117114
α-helix118-1192
β-strand120-124515
α-helix128-1303
β-strand131-132215
β-strand135-1451115
β-strand146114
β-strand151-154416
α-helix155-1573
β-strand159116
β-strand163-165315
α-helix166-1683
β-strand169-170215
β-strand176-1851015
β-strand194-200716
α-helix201-2033
β-strand205-211716
Chain E: 9 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand4-7417
β-strand10-14518
β-strand19-25717
β-strand27C119
β-strand31119
β-strand33-38618
β-strand45-49518
β-strand53-54218
α-helix551
β-strand62-67617
β-strand70-75617
α-helix80-823
β-strand84-90718
α-helix961
β-strand97-98218
β-strand102-107618
β-strand111120
α-helix112-1132
β-strand114-118521
α-helix119-1213
α-helix122-1265
β-strand129-1391121
β-strand140120
β-strand145-150622
β-strand153-154222
α-helix1551
β-strand159-163521
α-helix164-1674
β-strand173-1821021
α-helix183-1864
β-strand191-197722
β-strand205-210622

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
vFP7.04 heavy chainA, Dprotein221Mus musculus
vFP7.04 light chainB, Eprotein219Mus musculus
HIV fusion peptide (512-519)C, Fprotein8Human immunodeficiency virus 1Q2N0S5
Sequence of entity 1 (A, D), FASTA
>6CDM_1 vFP7.04 heavy chain (chains A, D)
QVQLQQSGAELVRPGASVTLSCKASGYTFTDYEMHWVKQTPVHGLEWIGAIVPETGFTAY
TQKFKGKAMLTADKSSSTAYMELRSLTSEDSAVYFCSRLRLYWYFDVWGTGTTVTVSSAS
TKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGL
YSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
Sequence of entity 2 (B, E), FASTA
>6CDM_2 vFP7.04 light chain (chains B, E)
GVLMTQTPLSLPVRLGDQASISCRSSQSIVYSNGNTYLEWYLQRPGQSPKLLIYKVSNRF
SGVPDRVSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPYTFGGGTKLEIKRTVAAPSV
FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 3 (C, F), FASTA
>6CDM_3 HIV fusion peptide (512-519) (chains C, F)
AVGIGAVF

Primary citation

Epitope-based vaccine design yields fusion peptide-directed antibodies that neutralize diverse strains of HIV-1. Xu, K., Acharya, P., Kong, R. et al. Nat Med (2018) 24:857-867. DOI 10.1038/s41591-018-0042-6 · PubMed

Other PDB entries of the same protein (UniProt Q2N0S5), best resolution first:

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