Research workbench
Myristoylated HIV-1 nef anchor domain, NMR, 2 structures
Analyse Myristoylated HIV-1 nef anchor domain, NMR, 2 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QA5
- Type
- protein
- Length
- 56 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (myristoylated HIV-1 nef anchor domain (myristate- GLY2 to TRP57))
- UniProt
- P04324
- Ligands
- MYR, NH2
Structure
solution nmr · 1 distinct chain · 18% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (myristoylated HIV-1 nef anchor domain (myristate- GLY2 to TRP57)) | protein | 56 | 18% helix, 0% strand | P04324 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 lipid (myristoylation).
Compared structures
- 1QA5 · Myristoylated HIV-1 nef anchor domain, NMR, 2 structures · 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 P04324
- Elsewhere: RCSB PDB 1QA5 · PDBe 1QA5 · UniProt P04324
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