MolNFT v1 · #160871 · protein
Structure of full-length, fully glycosylated, non-modified HIV-1 GP160 bound to PG16 Fab
6PWU: “Structure of full-length, fully glycosylated, non-modified HIV-1 GP160 bound to PG16 Fab”. Electron microscopy, 5 ligands (NAG, BMA, MAN). MolNFT v1 #160871 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PWU
- Type
- protein
- Length
- 2,301 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q71014
- Ligands
- NAG, BMA, MAN, FUC, GAL
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | — | protein | 615 | — | Q71014 |
| H | — | protein | 240 | — | — |
| L | — | protein | 216 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 109 copies · chains A, C, H, E, L
- BMA · beta-D-mannopyranose · sugar · 21 copies · chains A, L, E, H
- MAN · alpha-D-mannopyranose · sugar · 9 copies · chains H, L
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains C, A
- GAL · beta-D-galactopyranose · sugar · chains H, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PWU · Structure of full-length, fully glycosylated, non-modified HIV-1 gp160 bound to PG16 Fab · 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 Q71014
- Elsewhere: RCSB PDB 6PWU · PDBe 6PWU · UniProt Q71014
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.