Research workbench
CD4- and 17-bound HIV-1 env B41 sosip frozen with lmng
Analyse CD4- and 17-bound HIV-1 env B41 sosip frozen with lmng in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OPQ
- Type
- protein
- Length
- 2,535 residues
- Chains
- 15
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B3UES2, B3UEZ6, P01730
- Ligands
- NAG, MAN, BMA
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | — | protein | 385 | — | B3UES2 |
| L, N, O | — | protein | 108 | — | — |
| B, F, G | — | protein | 128 | — | B3UEZ6 |
| C, I, J | — | protein | 97 | — | P01730 |
| H, K, M | — | protein | 127 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 63 copies · chains A, D, E
- MAN · alpha-D-mannopyranose · sugar · 6 copies · chains A, D, E
- BMA · beta-D-mannopyranose · sugar · 3 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6OPQ · CD4- and 17-bound HIV-1 Env B41 SOSIP frozen with LMNG · the same entry in another collection · chain M against M, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt B3UES2
- Every structure of UniProt B3UEZ6
- Every structure of UniProt P01730
- Elsewhere: RCSB PDB 6OPQ · PDBe 6OPQ · UniProt B3UES2 · UniProt B3UEZ6 · UniProt P01730
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