8TTW: BG505 SOSIP.664 HIV-1 Env trimer

Cryo-EM structure of BG505 SOSIP.664 HIV-1 Env trimer in complex with temsavir, 8ANC195, and 10-1074. Determined by electron microscopy at 2.96 Å resolution. Released 8 Nov 2023.

Method: Electron microscopy
Resolution: 2.96 Å
Organisms: Human immunodeficiency virus 1, Homo sapiens
Chains: 18
Atoms: 31,275
Mol. weight: 539.16 kDa
Ligands: 83J, NAG
Released: 8 Nov 2023

Explore 8TTW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8TTW contains 89 α-helices and 363 β-strands across 18 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, 42 β-strands

Element	Residues	Length	Sheet
β-strand	35-40	6	1
β-strand	45-47	3	2
β-strand	53-55	3	3
β-strand	56	1	4
β-strand	67	1	5
α-helix	71-73	3
α-helix	75	1
β-strand	76	1	4
α-helix	77-78	2
β-strand	83-84	2	2
β-strand	91-94	4	6
α-helix	101-116	16
β-strand	121	1	7
α-helix	123-125	3
α-helix	128	1
β-strand	129-133	5	8
β-strand	154-161	8	8
β-strand	170-177	8	8
β-strand	181	1	9
β-strand	190-191	2	8
β-strand	193	1	9
β-strand	200-203	4	7
α-helix	204-205	2
β-strand	209	1	5
β-strand	215	1	10
β-strand	216-218	3	3
β-strand	223-228	6	2
β-strand	236-239	4	6
β-strand	242-245	4	2
β-strand	247	1	3
β-strand	251	1	10
β-strand	259-261	3	11
β-strand	271-274	4	11
β-strand	284-298	15	11
β-strand	304-312	7	12
β-strand	315-320	6	12
β-strand	330-334	5	11
α-helix	335-352	18
β-strand	358-361	4	11
β-strand	374-377	4	13
β-strand	382-385	4	13
β-strand	393-395	3	11
β-strand	413-416	4	11
β-strand	420-421	2	13
β-strand	423-425	3	7
β-strand	432-435	4	7
α-helix	437-439	3
β-strand	443-456	14	11
β-strand	465-470	6	11
α-helix	476-479	4
β-strand	486-491	6	2
β-strand	494-498	5	1

Chain B: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	524-526	3
β-strand	529	1	14
α-helix	532-534	3
α-helix	537-541	5
α-helix	570-584	15
α-helix	586-595	10
β-strand	603-609	7	1
β-strand	627	1	14
α-helix	628-635	8
α-helix	639-648	10
α-helix	653-660	8

Chain C: 2 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	15
β-strand	10-12	3	16
β-strand	18-25	8	15
β-strand	33-39	8	17
β-strand	45-51	7	17
β-strand	57-59	3	17
β-strand	67-72	6	15
β-strand	75	1	18
β-strand	77A	1	18
β-strand	77D-82	6	15
β-strand	89-96	8	17
β-strand	100E-100F	2	19
β-strand	100I-100J	2	19
β-strand	102-103	2	17
β-strand	109-111	3	16
β-strand	117	1	20
β-strand	121-124	4	21
β-strand	136-145	10	21
β-strand	146	1	20
β-strand	152-154	3	22
β-strand	159	1	22
β-strand	163-165	3	21
α-helix	166-168	3
β-strand	169-170	2	21
β-strand	176-184	9	21
α-helix	186-188	3
β-strand	194-198	5	22
β-strand	207-211	5	22

Chain D: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	23
β-strand	10	1	24
β-strand	19-25	7	23
β-strand	33-38	6	25
β-strand	46-49	4	25
β-strand	53-54	2	25
α-helix	55	1
β-strand	62-65	4	23
β-strand	70-75	6	23
β-strand	85-90	6	25
α-helix	96	1
β-strand	97-98	2	25
β-strand	103	1	24
β-strand	116-118	3	26
α-helix	119-121	3
α-helix	122-126	5
β-strand	129	1	27
β-strand	132-139	8	26
β-strand	145-150	6	28
β-strand	153-155	3	28
β-strand	159-163	5	26
α-helix	164-167	4
β-strand	173-179	7	26
β-strand	182	1	27
α-helix	183-188	6
β-strand	191-197	7	28
β-strand	205-210	6	28

Chain E: 8 helices, 41 β-strands

Element	Residues	Length	Sheet
β-strand	35-40	6	29
β-strand	45-47	3	30
β-strand	53-56	4	31
β-strand	67	1	32
α-helix	71-73	3
β-strand	75-76	2	31
α-helix	77-78	2
β-strand	83-86	4	30
β-strand	91-94	4	33
α-helix	99-116	18
β-strand	121	1	34
α-helix	123-125	3
α-helix	128	1
β-strand	129-133	5	35
β-strand	154-161	8	35
β-strand	170-177	8	35
β-strand	181	1	36
β-strand	190-191	2	35
β-strand	193	1	36
β-strand	200-203	4	34
α-helix	204-205	2
β-strand	209	1	32
β-strand	215	1	37
β-strand	216-218	3	31
β-strand	223-228	6	30
β-strand	236-239	4	33
β-strand	242-245	4	30
β-strand	247	1	31
β-strand	251	1	37
β-strand	259-261	3	38
β-strand	271-274	4	38
β-strand	284-298	15	38
β-strand	304-312	7	39
β-strand	315-320	6	39
β-strand	330-334	5	38
α-helix	335-352	18
β-strand	358-361	4	38
β-strand	374-378	5	40
β-strand	381-385	5	40
β-strand	394-395	2	38
β-strand	413-416	4	38
β-strand	420-421	2	40
β-strand	423-425	3	34
β-strand	432-435	4	34
α-helix	437-439	3
β-strand	443-456	14	38
β-strand	465-470	6	38
β-strand	486-491	6	30
β-strand	494-498	5	29

Chain F: 7 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	524-526	3
β-strand	529	1	41
α-helix	532-534	3
α-helix	537-541	5
α-helix	570-595	26
β-strand	603-609	7	29
β-strand	627	1	41
α-helix	628-635	8
α-helix	639-648	10
α-helix	653-660	8

Chains G and K: 2 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	42
β-strand	10-12	3	43
β-strand	18-25	8	42
β-strand	33-34	2	44
β-strand	35-39	6	45
β-strand	45-51	7	45
β-strand	57-59	3	45
β-strand	67-72	6	42
β-strand	75	1	46
β-strand	77A	1	46
β-strand	77D-82	6	42
β-strand	89-92	4	45
β-strand	93-94	2	47
β-strand	95-96	2	44
β-strand	100E-100F	2	48
β-strand	100I-100J	2	48
β-strand	102-103	2	47
β-strand	109-111	3	43
β-strand	117	1	49
β-strand	121-124	4	50
β-strand	136-145	10	50
β-strand	146	1	49
β-strand	152-154	3	51
β-strand	159	1	51
β-strand	163-165	3	50
α-helix	166-168	3
β-strand	169-170	2	50
β-strand	176-184	9	50
α-helix	186-188	3
β-strand	194-198	5	51
β-strand	207-211	5	51

Chain H: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	52
β-strand	10	1	53
β-strand	19-24	6	52
β-strand	33-38	6	54
β-strand	46-49	4	54
β-strand	53-54	2	54
α-helix	55	1
β-strand	62-65	4	52
β-strand	70-75	6	52
β-strand	85-90	6	54
α-helix	96	1
β-strand	97-98	2	54
β-strand	103	1	53
β-strand	116-118	3	55
α-helix	119-121	3
α-helix	122-126	5
β-strand	129	1	56
β-strand	132-139	8	55
β-strand	145-150	6	57
β-strand	153-155	3	57
β-strand	159-163	5	55
α-helix	164-167	4
β-strand	173-179	7	55
β-strand	182	1	56
α-helix	183-188	6
β-strand	191-197	7	57
β-strand	206-210	5	57

9 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Envelope glycoprotein gp160	A, E, I	protein	481	Human immunodeficiency virus 1	Q2N0S6
BG505 SOSIP.664 transmembrane protein gp41	B, F, J	protein	153	Human immunodeficiency virus 1	Q2N0S5
Antibody 8anc195 heavy chain	C, G, K	protein	238	Homo sapiens
Antibody 8anc195 light chain	D, H, L	protein	215	Homo sapiens
Antibody 10-1074 heavy chain	M, O, Q	protein	238	Homo sapiens
Antibody 10-1074 light chain	N, P, R	protein	214	Homo sapiens

Sequence of entity 1 (A, E, I), FASTA

>8TTW_1 Envelope glycoprotein gp160 (chains A, E, I)
AENLWVTVYYGVPVWKDAETTLFCASDAKAYETEKHNVWATHACVPTDPNPQEIHLENVT
EEFNMWKNNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLQCTNVTNNITDDMRGELKNCS
FNMTTELRDKKQKVYSLFYRLDVVQINENQGNRSNNSNKEYRLINCNTSAITQACPKVSF
EPIPIHYCAPAGFAILKCKDKKFNGTGPCPSVSTVQCTHGIKPVVSTQLLLNGSLAEEEV
MIRSENITNNAKNILVQFNTPVQINCTRPNNNTRKSIRIGPGQAFYATGDIIGDIRQAHC
NVSKATWNETLGKVVKQLRKHFGNNTIIRFANSSGGDLEVTTHSFNCGGEFFYCNTSGLF
NSTWISNTSVQGSNSTGSNDSITLPCRIKQIINMWQRIGQAMYAPPIQGVIRCVSNITGL
ILTRDGGSTNSTTETFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTRCKRRVVGRRRRR
R

Sequence of entity 2 (B, F, J), FASTA

>8TTW_2 BG505 SOSIP.664 transmembrane protein gp41 (chains B, F, J)
AVGIGAVFLGFLGAAGSTMGAASMTLTVQARNLLSGIVQQQSNLLRAPEAQQHLLKLTVW
GIKQLQARVLAVERYLRDQQLLGIWGCSGKLICCTNVPWNSSWSNRNLSEIWDNMTWLQW
DKEISNYTQIIYGLLEESQNQQEKNEQDLLALD

Sequence of entity 3 (C, G, K), FASTA

>8TTW_3 Antibody 8anc195 heavy chain (chains C, G, K)
QIHLVQSGTEVKKPGSSVTVSCKAYGVNTFGLYAVNWVRQAPGQSLEYIGQIWRWKSSAS
HHFRGRVLISAVDLTGSSPPISSLEIKNLTSDDTAVYFCTTTSTYDRWSGLHHDGVMAFS
SWGQGTLISVSAASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTS
GVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKT

Sequence of entity 4 (D, H, L), FASTA

>8TTW_4 Antibody 8anc195 light chain (chains D, H, L)
DIQMTQSPSTLSASTGDTVRISCRASQSITGNWVAWYQQRPGKAPRLLIYRGAALLGGVP
SRFRGSAAGTDFTLTIGNLQAEDFGTFYCQQYDTYPGTFGQGTKVEVKRTVAAPSVFIFP
PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 5 (M, O, Q), FASTA

>8TTW_5 Antibody 10-1074 heavy chain (chains M, O, Q)
QVQLQESGPGLVKPSETLSVTCSVSGDSMNNYYWTWIRQSPGKGLEWIGYISDRESATYN
PSLNSRVVISRDTSKNQLSLKLNSVTPADTAVYYCATARRGQRIYGVVSFGEFFYYYSMD
VWGKGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTS
GVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKT

Sequence of entity 6 (N, P, R), FASTA

>8TTW_6 Antibody 10-1074 light chain (chains N, P, R)
SYVRPLSVALGETARISCGRQALGSRAVQWYQHRPGQAPILLIYNNQDRPSGIPERFSGT
PDINFGTRATLTISGVEAGDEADYYCHMWDSRSGFSWSFGGATRLTVLGQPKAAPSVTLF
PPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYL
SLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS

Ligands and cofactors

ID	Name	Formula	Copies
83J	1-[4-(benzenecarbonyl)piperazin-1-yl]-2-[4-methoxy-7-(3-methyl-1H-1,2,4-triazol…	C24 H23 N7 O4	3
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	21

Primary citation

Structure-function analyses reveal key molecular determinants of HIV-1 CRF01_AE resistance to the entry inhibitor temsavir. Prevost, J., Chen, Y., Zhou, F. et al. Nat Commun (2023) 14:6710-6710. DOI 10.1038/s41467-023-42500-2 · PubMed

Other PDB entries of the same protein (UniProt Q2N0S6), best resolution first:

8TOX 2.3 Å, Cryo-EM structure of BG505 Env mutant A517E in complex with antibody ACS202 Fab
6MTJ 2.34 Å, Crystal Structure of HIV-1 BG505 SOSIP.664 Prefusion Env Trimer Bound to Small Molecule…
6W03 2.4 Å, Crystal Structure of HIV-1 BG505 DS-SOSIP.3mut Prefusion Env Trimer in Complex with…
6MTN 2.5 Å, Crystal Structure of HIV-1 BG505 SOSIP.664 Prefusion Env Trimer Bound to Small Molecule…
6UDJ 2.5 Å, HIV-1 bNAb 1-18 in complex with BG505 SOSIP.664 and 10-1074
8FR6 2.5 Å, Antibody vFP53.02 in complex with HIV-1 envelope trimer BG505 DS-SOSIP
6MU7 2.5 Å, Crystal Structure of HIV-1 BG505 SOSIP.664 Prefusion Env Trimer Bound to Small Molecule…
6MU6 2.55 Å, Crystal Structure of HIV-1 BG505 SOSIP.664 Prefusion Env Trimer Bound to Small Molecule…
6NNJ 2.6 Å, Crystal Structure of HIV-1 BG505 SOSIP.664 Prefusion Env Trimer Bound to CH31 scFv in…
8EUV 2.6 Å, Cryo-EM structure of HIV-1 BG505 DS-SOSIP ENV trimer bound to VRC34.01-COMBO1 FAB
8T4K 2.6 Å, MD64 N332-GT5 sosip
8EUU 2.7 Å, Cryo-EM structure of HIV-1 BG505 DS-SOSIP ENV trimer bound to VRC34.01 FAB

Browse structure collections

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