Research workbench
Assembly of viqki I454(BETA-L-HOMOISOLEUCINE)WITH human parainfluenza virus type 3 (HPIV3) fusion glycoprotein N-terminal heptad repeat domain
Analyse Assembly of viqki I454(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
- 6VAS
- Type
- protein
- Length
- 120 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P06828
- Ligands
- NH2
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 44 | — | P06828 |
| B | — | protein | 30 | — | P06828 |
| C | — | protein | 24 | — | P06828 |
| D | — | protein | 22 | — | P06828 |
Ligands and binding sites
- NH2 · Amino group · ion · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VAS · Assembly of VIQKI I454(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 6VAS · PDBe 6VAS · UniProt P06828
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