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Assembly of viqki I456(BETA-L-HOMOISOLEUCINE)WITH human parainfluenza virus type 3 (HPIV3) fusion glycoprotein N-terminal heptad repeat domain
Analyse Assembly of viqki I456(BETA-L-HOMOISOLEUCINE)WITH human parainfluenza virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V3V
- Type
- protein
- Length
- 246 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion glycoprotein F1
- UniProt
- P06828
- Ligands
- NH2
Structure
x-ray diffraction · 5 distinct chains · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fusion glycoprotein F1 | protein | 47 | 94% helix, 0% strand | P06828 |
| B, D | Fusion glycoprotein F1 | protein | 34 | 79% helix, 0% strand | P06828 |
| C | Fusion glycoprotein F1 | protein | 49 | 94% helix, 0% strand | P06828 |
| E | Fusion glycoprotein F1 | protein | 46 | 89% helix, 0% strand | P06828 |
| F | Fusion glycoprotein F1 | protein | 36 | 75% helix, 0% strand | P06828 |
Ligands and binding sites
- NH2 · Amino group · ion · 2 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
9 interfaces between chains.
- C–F · 1009 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 952 Ų buried · 9 hydrogen bonds · protein-protein
- B–E · 938 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 908 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 864 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (nonstandard).
Compared structures
- 6V3V · Assembly of VIQKI I456(beta-L-homoisoleucine)with human parainfluenza virus type 3… · 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 6V3V · PDBe 6V3V · UniProt P06828
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