MolNFT v1 · #147372 · protein
Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop
6EAY: “Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion…”. X-ray diffraction, 3 ligands (MAN, NAG, BMA). MolNFT v1 #147372 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6EAY
- Type
- protein
- Length
- 747 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q05320
- Ligands
- MAN, NAG, BMA
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 211 | — | — |
| H | — | protein | 202 | — | — |
| A | — | protein | 113 | — | Q05320 |
| B | — | protein | 221 | — | Q05320 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 5 copies · chains B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6EAY · Structural Basis for Broad Neutralization of Ebolaviruses by an Antibody Targeting the… · the same entry in another collection · chain L against L, 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 Q05320
- Elsewhere: RCSB PDB 6EAY · PDBe 6EAY · UniProt Q05320
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