Research workbench
Solution structure of the M-pmv myristoylated matrix protein
Analyse Solution structure of the M-pmv myristoylated matrix protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LMY
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Matrix protein P10
- UniProt
- P07567
- Ligands
- MYR
- Pockets
- 2 · best druggability 0.66
Structure
solution nmr · 1 distinct chain · 55% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Matrix protein P10 | protein | 124 | 55% helix, 0% strand | P07567 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 365 | 0.66 | 0.80 | 40 | MYR |
| 2 | 330 | 0.65 | 0.80 | 30 | empty |
Modifications
Observed in the structure: 1 lipid (myristoylation).
Compared structures
- 5LMY · Solution structure of the m-pmv myristoylated 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 P07567
- Elsewhere: RCSB PDB 5LMY · PDBe 5LMY · UniProt P07567
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