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Conformational mapping of the N-terminal fusion peptide of HIV-1 GP41 using 13C-enhanced fourier transform infrared spectroscopy (ftir)
Analyse Conformational mapping of the N-terminal fusion peptide of HIV-1 GP41 using… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ERF
- Type
- protein
- Length
- 23 residues
- Chains
- 1
- Method
- infrared spectroscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transmembrane glycoprotein
- UniProt
- P03377
- Ligands
- NH2
Structure
infrared spectroscopy · 1 distinct chain · 57% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transmembrane glycoprotein | protein | 23 | 57% helix, 0% strand | P03377 |
Ligands and binding sites
- NH2 · Amino group · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1ERF · Conformational mapping of the N-terminal fusion peptide of HIV-1 GP41 using 13C-enhanced… · 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 P03377
- Elsewhere: RCSB PDB 1ERF · PDBe 1ERF · UniProt P03377
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