Research workbench
Structure of the uncleaved paramyxovirus (HPIV3) fusion protein
Analyse Structure of the uncleaved paramyxovirus (HPIV3) fusion protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZTM
- Type
- protein
- Length
- 1,258 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion glycoprotein
- UniProt
- P06828
- Ligands
- NAG
- Pockets
- 14 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fusion glycoprotein | protein | 416 | 38% helix, 25% strand | P06828 |
| B | Fusion glycoprotein | protein | 418 | 37% helix, 26% strand | P06828 |
| C | Fusion glycoprotein | protein | 424 | 38% helix, 25% strand | P06828 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.68 | 0.77 | 78 | empty |
| 2 | 532 | 0.68 | 0.78 | 58 | empty |
| 3 | 611 | 0.67 | 0.77 | 63 | empty |
| 4 | 77 | 0.65 | 0.93 | 18 | empty |
| 5 | 353 | 0.64 | 0.79 | 56 | empty |
Interfaces
3 interfaces between chains.
- A–B · 5604 Ų buried · 55 hydrogen bonds · protein-protein
- B–C · 5591 Ų buried · 57 hydrogen bonds · protein-protein
- A–C · 5493 Ų buried · 51 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 1ZTM · Structure of the Uncleaved Paramyxovirus (hPIV3) Fusion Protein · 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 P06828
- Elsewhere: RCSB PDB 1ZTM · PDBe 1ZTM · UniProt P06828
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