Research workbench
Crystal structure of human metapneumovirus fusion glycoprotein stabilized in the prefusion state
Analyse Crystal structure of human metapneumovirus fusion glycoprotein stabilized in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WB0
- Type
- protein
- Length
- 442 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion glycoprotein F0
- UniProt
- Q1A2Z0
- Ligands
- NAG, BMA, MAN, SO4
- Pockets
- 5 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F | Fusion glycoprotein F0 | protein | 442 | 32% helix, 34% strand | Q1A2Z0 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains F
- BMA · beta-D-mannopyranose · sugar
- MAN · alpha-D-mannopyranose · sugar
- SO4 · Sulfate ion · ion · 4 copies · chains F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.52 | 0.80 | 22 | empty |
| 2 | 52 | 0.41 | 0.82 | 15 | empty |
| 3 | 100 | 0.36 | 0.75 | 20 | empty |
| 4 | 68 | 0.28 | 0.72 | 17 | empty |
| 5 | 50 | 0.27 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 7 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 5WB0 · Crystal structure of human metapneumovirus fusion glycoprotein stabilized in the… · 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 Q1A2Z0
- Elsewhere: RCSB PDB 5WB0 · PDBe 5WB0 · UniProt Q1A2Z0
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