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Crystal structure of a human metapneumovirus monomeric fusion protein complexed with 458 Fab
Analyse Crystal structure of a human metapneumovirus monomeric fusion protein complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W16
- Type
- protein
- Length
- 818 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6W8S4, M1E1E4
- Ligands
- NAG, MAN, BMA
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F | — | protein | 385 | — | Q6W8S4, M1E1E4 |
| H | — | protein | 219 | — | — |
| L | — | protein | 214 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains F, L
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains L
- BMA · beta-D-mannopyranose · sugar · chains L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6W16 · Crystal structure of a human metapneumovirus monomeric fusion protein complexed with 458… · the same entry in another collection · chain F against F, 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 Q6W8S4
- Every structure of UniProt M1E1E4
- Elsewhere: RCSB PDB 6W16 · PDBe 6W16 · UniProt Q6W8S4 · UniProt M1E1E4
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