Research workbench
NMR structure of the myristylated feline immunodeficiency virus matrix protein
Analyse NMR structure of the myristylated feline immunodeficiency virus matrix protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N1R
- Type
- protein
- Length
- 134 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Matrix protein P15
- UniProt
- P16087
- Ligands
- MYR
- Pockets
- 2 · best druggability 0.53
Structure
solution nmr · 1 distinct chain · 53% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Matrix protein P15 | protein | 134 | 53% helix, 2% strand | P16087 |
Ligands and binding sites
- MYR · Myristic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.53 | 0.78 | 31 | empty |
| 2 | 102 | 0.41 | 0.77 | 20 | MYR |
Modifications
Observed in the structure: 1 lipid (myristoylation).
Compared structures
- 2N1R · NMR Structure of the Myristylated Feline Immunodeficiency Virus Matrix Protein · 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 P16087
- Elsewhere: RCSB PDB 2N1R · PDBe 2N1R · UniProt P16087
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.