Research workbench
BG505 MD64 N332-GT2 sosip trimer in complex with germline-reverted BG18 fragment antigen binding
Analyse BG505 MD64 N332-GT2 sosip trimer in complex with germline-reverted BG18… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DFH
- Type
- protein
- Length
- 2,406 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2N0S6, Q2N0S5
- 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 | 128 | — | Q2N0S5 |
| H, G, I | — | protein | 128 | — | — |
| L, J, K | — | protein | 106 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 66 copies · chains A, H, C, G, D, I, B, E, F
- MAN · alpha-D-mannopyranose · sugar · 18 copies · chains A, H, C, G, D, I
- BMA · beta-D-mannopyranose · sugar · 6 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6DFH · BG505 MD64 N332-GT2 SOSIP trimer in complex with germline-reverted BG18 fragment antigen… · 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
- Every structure of UniProt Q2N0S5
- Elsewhere: RCSB PDB 6DFH · PDBe 6DFH · UniProt Q2N0S6 · UniProt Q2N0S5
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