Research workbench
Complex of a chimeric ALPHA/BETA-peptide based on the GP41 chr domain bound to a GP41 nhr domain peptide
Analyse Complex of a chimeric ALPHA/BETA-peptide based on the GP41 chr domain bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O3Z
- Type
- protein
- Length
- 68 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelope glycoprotein GP160; Chimeric ALPHA/BETA peptide based on GP41 chr domain sequence
- UniProt
- Q9YP39
- Ligands
- ACE
Structure
x-ray diffraction · 2 distinct chains · 90% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Envelope glycoprotein GP160 | protein | 32 | 91% helix, 0% strand | Q9YP39 |
| B | Chimeric ALPHA/BETA peptide based on GP41 chr domain sequence | protein | 36 | 89% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 496 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified, 1 covalent (nonstandard, covalent ligand).
Compared structures
- 3O3Z · Complex of a chimeric alpha/beta-peptide based on the gp41 CHR domain bound to a gp41 NHR… · 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 Q9YP39
- Elsewhere: RCSB PDB 3O3Z · PDBe 3O3Z · UniProt Q9YP39
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