MolNFT v1 · #169369 · protein
HIV-1 envelope glycoprotein BG505 SOSIP.664 expressed in stable cho cells in complex with RM20A3 Fab
6X9S · HIV-1 envelope glycoprotein BG505 SOSIP.664 GP120: “HIV-1 envelope glycoprotein BG505 SOSIP.664 expressed in stable cho cells in complex with RM20A3 Fab”. Electron microscopy, 3 ligands (NAG, BMA, MAN), 11 pockets (best druggability…
- PDB
- 6X9S
- Type
- protein
- Length
- 786 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV-1 envelope glycoprotein BG505 SOSIP.664 GP120; HIV-1 envelope glycoprotein BG505…
- UniProt
- Q2N0S6
- Ligands
- NAG, BMA, MAN
- Pockets
- 11 · best druggability 0.70
Structure
electron microscopy · 4 distinct chains · 19% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HIV-1 envelope glycoprotein BG505 SOSIP.664 GP120 | protein | 432 | 14% helix, 44% strand | Q2N0S6 |
| B | HIV-1 envelope glycoprotein BG505 SOSIP.664 GP41 | protein | 121 | 61% helix, 4% strand | Q2N0S6 |
| H | RM20A3 Fab heavy chain | protein | 124 | 7% helix, 50% strand | — |
| L | RM20A3 Fab light chain | protein | 109 | 7% helix, 43% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 27 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar
- MAN · alpha-D-mannopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 326 | 0.70 | 0.83 | 53 | NAG |
| 2 | 63 | 0.66 | 0.94 | 25 | empty |
| 3 | 159 | 0.56 | 0.81 | 30 | empty |
| 4 | 234 | 0.52 | 0.76 | 39 | empty |
| 5 | 117 | 0.46 | 0.78 | 20 | empty |
Interfaces
4 interfaces between chains.
- A–B · 2390 Ų buried · 20 hydrogen bonds · protein-protein
- H–L · 903 Ų buried · 3 hydrogen bonds · protein-protein
- A–H · 176 Ų buried · 4 hydrogen bonds · protein-protein
- B–H · 171 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 glycan, 12 disulfide (N-glycosylation, disulfide).
Compared structures
- 6X9S · HIV-1 Envelope Glycoprotein BG505 SOSIP.664 expressed in stable CHO cells in complex with… · 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 6X9S · PDBe 6X9S · UniProt Q2N0S6
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