6OPP: 17b Fab light chain
Asymmetric model of CD4- and 17-bound B41 HIV-1 Env SOSIP in complex with DDM. Determined by electron microscopy at 3.7 Å resolution. Released 21 Oct 2020.
- Method
- Electron microscopy
- Resolution
- 3.7 Å
- Organisms
- Homo sapiens, Human immunodeficiency virus 1
- Chains
- 15
- Atoms
- 21,852
- Mol. weight
- 467.58 kDa
- Ligands
- NAG, LMT
- Released
- 21 Oct 2020
Explore 6OPP in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6OPP contains 79 α-helices and 201 β-strands across 15 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: 12 helices, 32 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 35-40 | 6 | 4 |
| β-strand | 45-47 | 3 | 5 |
| α-helix | 51-52 | 2 | |
| β-strand | 53-55 | 3 | 6 |
| α-helix | 65-73 | 9 | |
| β-strand | 75 | 1 | 6 |
| α-helix | 76-78 | 3 | |
| β-strand | 83-85 | 3 | 5 |
| β-strand | 91-94 | 4 | 7 |
| α-helix | 95-97 | 3 | |
| α-helix | 100-115 | 16 | |
| β-strand | 120-126 | 7 | 8 |
| β-strand | 196-202 | 7 | 8 |
| β-strand | 215 | 1 | 9 |
| β-strand | 216-218 | 3 | 6 |
| α-helix | 219-220 | 2 | |
| β-strand | 223-228 | 6 | 5 |
| β-strand | 236-239 | 4 | 7 |
| β-strand | 242-245 | 4 | 5 |
| β-strand | 247 | 1 | 6 |
| α-helix | 248-250 | 3 | |
| β-strand | 251 | 1 | 9 |
| β-strand | 259-261 | 3 | 10 |
| β-strand | 271-273 | 3 | 10 |
| α-helix | 283 | 1 | |
| β-strand | 284-298 | 15 | 10 |
| β-strand | 328-334 | 7 | 10 |
| α-helix | 335-349 | 15 | |
| β-strand | 357-361 | 4 | 10 |
| β-strand | 367 | 1 | 11 |
| α-helix | 369-372 | 4 | |
| β-strand | 374-378 | 5 | 10 |
| β-strand | 381-385 | 5 | 10 |
| β-strand | 394-395 | 2 | 10 |
| β-strand | 400 | 1 | 10 |
| β-strand | 413-421 | 9 | 10 |
| β-strand | 423-425 | 3 | 8 |
| β-strand | 432-434 | 3 | 8 |
| α-helix | 436-439 | 4 | |
| β-strand | 443-457 | 15 | 10 |
| β-strand | 465-470 | 6 | 10 |
| α-helix | 475-483 | 9 | |
| β-strand | 486-491 | 6 | 5 |
| β-strand | 494-499 | 6 | 4 |
Chain B: 8 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 529 | 1 | 3 |
| α-helix | 530-545 | 16 | |
| α-helix | 568-592 | 25 | |
| α-helix | 593-596 | 4 | |
| β-strand | 603-609 | 7 | 4 |
| α-helix | 610-611 | 2 | |
| α-helix | 619-625 | 7 | |
| β-strand | 627 | 1 | 3 |
| α-helix | 628-634 | 7 | |
| α-helix | 636-638 | 3 | |
| α-helix | 639-663 | 25 | |
Chain C: 2 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-5 | 4 | 11 |
| β-strand | 12-17 | 6 | 12 |
| β-strand | 26-29 | 4 | 11 |
| β-strand | 35-40 | 6 | 11 |
| β-strand | 43-46 | 4 | 11 |
| β-strand | 55-56 | 2 | 12 |
| α-helix | 59-64 | 6 | |
| β-strand | 66-71 | 6 | 12 |
| α-helix | 76-78 | 3 | |
| β-strand | 81-86 | 6 | 11 |
| β-strand | 89 | 1 | 11 |
| β-strand | 92-96 | 5 | 11 |
Chain D: 10 helices, 34 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 35-40 | 6 | 17 |
| β-strand | 45-47 | 3 | 18 |
| α-helix | 51-52 | 2 | |
| β-strand | 53-55 | 3 | 19 |
| α-helix | 65-73 | 9 | |
| β-strand | 75 | 1 | 19 |
| α-helix | 76-77 | 2 | |
| β-strand | 83-85 | 3 | 18 |
| β-strand | 91-94 | 4 | 20 |
| α-helix | 99-113 | 15 | |
| β-strand | 120-123 | 4 | 21 |
| β-strand | 126 | 1 | 22 |
| β-strand | 196 | 1 | 22 |
| β-strand | 199-202 | 4 | 21 |
| β-strand | 215 | 1 | 23 |
| β-strand | 216-218 | 3 | 19 |
| α-helix | 219-220 | 2 | |
| β-strand | 223-228 | 6 | 18 |
| β-strand | 236-239 | 4 | 20 |
| β-strand | 242-245 | 4 | 18 |
| β-strand | 247 | 1 | 19 |
| α-helix | 248-250 | 3 | |
| β-strand | 251 | 1 | 23 |
| β-strand | 259-260 | 2 | 24 |
| β-strand | 271-274 | 4 | 24 |
| β-strand | 283-298 | 16 | 24 |
| β-strand | 328-334 | 7 | 24 |
| α-helix | 335-349 | 15 | |
| β-strand | 357-361 | 4 | 24 |
| β-strand | 367 | 1 | 25 |
| α-helix | 369-372 | 4 | |
| β-strand | 374-378 | 5 | 24 |
| β-strand | 381-385 | 5 | 24 |
| β-strand | 394-395 | 2 | 24 |
| β-strand | 400 | 1 | 24 |
| β-strand | 413-421 | 9 | 24 |
| β-strand | 423-425 | 3 | 21 |
| β-strand | 432-434 | 3 | 21 |
| α-helix | 436-439 | 4 | |
| β-strand | 443-457 | 15 | 24 |
| β-strand | 465-470 | 6 | 24 |
| α-helix | 475-483 | 9 | |
| β-strand | 486-491 | 6 | 18 |
| β-strand | 494-499 | 6 | 17 |
Chain E: 8 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 529 | 1 | 26 |
| α-helix | 530-546 | 17 | |
| α-helix | 568-592 | 25 | |
| α-helix | 593-596 | 4 | |
| β-strand | 603-609 | 7 | 17 |
| α-helix | 610-611 | 2 | |
| α-helix | 619-625 | 7 | |
| β-strand | 627 | 1 | 26 |
| α-helix | 628-634 | 7 | |
| α-helix | 636-638 | 3 | |
| α-helix | 639-660 | 22 | |
Chain F: 2 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-5 | 4 | 25 |
| β-strand | 12-17 | 6 | 45 |
| β-strand | 26-29 | 4 | 25 |
| β-strand | 35-40 | 6 | 25 |
| β-strand | 43-46 | 4 | 25 |
| β-strand | 55-56 | 2 | 45 |
| α-helix | 59-64 | 6 | |
| β-strand | 66-71 | 6 | 45 |
| α-helix | 76-78 | 3 | |
| β-strand | 81-86 | 6 | 25 |
| β-strand | 89-96 | 8 | 25 |
Chain G: 4 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 27 |
| β-strand | 10-12 | 3 | 28 |
| β-strand | 18-25 | 8 | 27 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 28 |
| β-strand | 45-52 | 8 | 28 |
| β-strand | 56-59 | 4 | 28 |
| β-strand | 67-72 | 6 | 27 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 27 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 28 |
| α-helix | 100-100B | 3 | |
| β-strand | 102-103 | 2 | 28 |
| β-strand | 107-111 | 5 | 28 |
Chain H: 3 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 13 |
| β-strand | 10-12 | 3 | 14 |
| β-strand | 18-25 | 8 | 13 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 14 |
| β-strand | 45-52 | 8 | 14 |
| β-strand | 56-59 | 4 | 14 |
| β-strand | 67-72 | 6 | 13 |
| β-strand | 77-82 | 6 | 13 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 14 |
| α-helix | 100-100B | 3 | |
| β-strand | 102-103 | 2 | 14 |
| β-strand | 107-111 | 5 | 14 |
7 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 |
|---|
| 17b Fab light chain | I, L, O | protein | 214 | Homo sapiens | |
| Envelope glycoprotein gp41 | B, E, K | protein | 153 | Human immunodeficiency virus 1 | B3UEZ6 |
| Envelope glycoprotein gp160 | A, D, J | protein | 524 | Human immunodeficiency virus 1 | B3UES2 |
| T-cell surface glycoprotein CD4 | C, F, M | protein | 208 | Homo sapiens | P01730 (AlphaFold model) |
| 17b Fab heavy chain | G, H, N | protein | 229 | Homo sapiens | |
Sequence of entity 1 (I, L, O), FASTA
>6OPP_1 17b Fab light chain (chains I, L, O)
ELELTQSPATLSVSPGERATLSCRASESVSSDLAWYQQKPGQAPRLLIYGASTRATGVPA
RFSGSGSGAEFTLTISSLQSEDFAVYYCQQYNNWPPRYTFGQGTRLEIKRTVAAPSVFIF
PPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSST
LTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRG
Sequence of entity 2 (B, E, K), FASTA
>6OPP_2 Envelope glycoprotein gp41 (chains B, E, K)
AVGLGAFILGFLGAAGSTMGAASMALTVQARLLLSGIVQQQNNLLRAPEAQQHMLQLTVW
GIKQLQARVLAVERYLRDQQLLGIWGCSGKIICCTNVPWNDSWSNKTINEIWDNMTWMQW
EKEIDNYTQHIYTLLEVSQIQQEKNEQELLELD
Sequence of entity 3 (A, D, J), FASTA
>6OPP_3 Envelope glycoprotein gp160 (chains A, D, J)
MDAMKRGLCCVLLLCGAVFVSPSQEIHARFRRGARAAKKWVTVYYGVPVWKEATTTLFCA
SDAKAYDTEVHNVWATHACVPTDPNPQEIVLGNVTENFNMWKNNMVEQMHEDIISLWDQS
LKPCVKLTPLCVTLNCNNVNTNNTNNSTNATISDWEKMETGEMKNCSFNVTTSIRDKIKK
EYALFYKLDVVPLENKNNINNTNITNYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFA
ILKCNSKTFNGSGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIVIRSENITDNAKTI
IVQLNEAVEINCTRPNNNTRKSIHIGPGRAFYATGDIIGNIRQAHCNISKARWNETLGQI
VAKLEEQFPNKTIIFNHSSGGDPEIVTHSFNCGGEFFYCNTTPLFNSTWNNTRTDDYPTG
GEQNITLQCRIKQIINMWQGVGKAMYAPPIRGQIRCSSNITGLLLTRDGGRDQNGTETFR
PGGGNMRDNWRSELYKYKVVKIEPLGIAPTACKRRVVQRRRRRR
Sequence of entity 4 (C, F, M), FASTA
>6OPP_4 T-cell surface glycoprotein CD4 (chains C, F, M)
METDTLLLWVLLLWVPGSTGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQ
GSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGL
TANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCT
VLQNQKKVEFKIDIVVLAGGSGHHHHHH
Sequence of entity 5 (G, H, N), FASTA
>6OPP_5 17b Fab heavy chain (chains G, H, N)
QVQLLESGAEVKKPGSSVKVSCKASGDTFIRYSFTWVRQAPGQGLEWMGRIITILDVAHY
APHLQGRVTITADKSTSTVYLELRNLRSDDTAVYFCAGVYEGEADEGEYDNNGFLKHWGQ
GTLVTVTSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHT
FPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 24 |
| LMT | Dodecyl-beta-D-maltoside | C24 H46 O11 | 3 |
Primary citation
A Strain-Specific Inhibitor of Receptor-Bound HIV-1 Targets a Pocket near the Fusion Peptide. Ozorowski, G., Torres, J.L., Santos-Martins, D. et al. Cell Rep (2020) 33:108428-108428. DOI 10.1016/j.celrep.2020.108428 · PubMed
Other PDB entries of the same protein (UniProt B3UEZ6), best resolution first:
- 6MUF 2.91 Å, Crystal Structure of HIV-1 B41 SOSIP.664 Prefusion Env Trimer in Complex with Human…
- 6MUG 2.95 Å, Crystal Structure of HIV-1 B41 SOSIP.664 Prefusion Env Trimer Bound to Small Molecule…
- 6OKP 3.28 Å, B41 SOSIP.664 in complex with the silent-face antibody SF12 and V3-targeting antibody…
- 6OPN 3.5 Å, CD4- and 17-bound HIV-1 Env B41 SOSIP in complex with small molecule GO35
- 6OPO 3.5 Å, Symmetric model of CD4- and 17-bound B41 HIV-1 Env SOSIP in complex with DDM
- 5VN8 3.6 Å, Cryo-EM model of B41 SOSIP.664 in complex with fragment antigen binding variable domain…
- 6X5B 3.6 Å, Symmetric model of CD4- and 17-bound B41 HIV-1 Env SOSIP in complex with small molecule…
- 5VN3 3.7 Å, Cryo-EM model of B41 SOSIP.664 in complex with soluble CD4 (D1-D2) and fragment antigen…
- 6OPQ 3.8 Å, CD4- and 17-bound HIV-1 Env B41 SOSIP frozen with LMNG
- 6U59 3.86 Å, HIV-1 B41 SOSIP.664 in complex with rabbit antibody 13B
- 6X5C 4.04 Å, Asymmetric model of CD4-bound B41 HIV-1 Env SOSIP in complex with small molecule GO52
- 6EDU 4.06 Å, B41 SOSIP.664 in complex with soluble CD4 (D1-D2), the co-receptor mimicking antibody…
Browse structure collections
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