Research workbench
Structure of full-length, fully glycosylated, non-modified HIV-1 GP160 bound to PG16 Fab at a nominal resolution of 4.6 ångström
Analyse Structure of full-length, fully glycosylated, non-modified HIV-1 GP160 bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ULC
- Type
- protein
- Length
- 2,301 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q71014
- Ligands
- NAG, BMA, MAN, FUC, GAL
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | — | protein | 471 | — | Q71014 |
| B, D, F | — | protein | 144 | — | Q71014 |
| H | — | protein | 240 | — | — |
| L | — | protein | 216 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 109 copies · chains A, H, C, B, E, F, L, D
- BMA · beta-D-mannopyranose · sugar · 21 copies · chains H, L
- 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
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ULC · 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 6ULC · PDBe 6ULC · UniProt Q71014
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