MolNFT v1 · #167540 · protein
BG505 SOSIP.V5.2 in complex with rhesus macaque Fab RM20J
6VO1: “BG505 SOSIP.V5.2 in complex with rhesus macaque Fab RM20J”. Electron microscopy, 3 ligands (NAG, MAN, BMA). MolNFT v1 #167540 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6VO1
- Type
- protein
- Length
- 2,382 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2N0S6
- Ligands
- NAG, MAN, BMA
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | — | protein | 440 | — | Q2N0S6 |
| B, E, F | — | protein | 129 | — | Q2N0S6 |
| H, G, I | — | protein | 118 | — | — |
| L, J, K | — | protein | 107 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 72 copies · chains A, B, C, E, D, F
- MAN · alpha-D-mannopyranose · sugar · 9 copies · chains A, C, D
- BMA · beta-D-mannopyranose · sugar · 6 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VO1 · BG505 SOSIP.v5.2 in complex with rhesus macaque Fab RM20J · the same entry in another collection · chain A against A, 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 Q2N0S6
- Elsewhere: RCSB PDB 6VO1 · PDBe 6VO1 · UniProt Q2N0S6
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