MolNFT v1 · #161406 · protein
Molecular features of the unc-45 chaperone critical for binding and folding muscle myosin
6QDJ · Myosin-4: “Molecular features of the unc-45 chaperone critical for binding and folding muscle myosin”. X-ray diffraction, 2 ligands (ADP, P15), 7 pockets (best druggability 0.79). MolNFT v1 #161406 on GenesisL1: 3D structure…
- PDB
- 6QDJ
- Type
- protein
- Length
- 758 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin-4
- UniProt
- P02566
- Ligands
- ADP, P15
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin-4 | protein | 758 | 48% helix, 15% strand | P02566 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- P15 · 2,5,8,11,14,17-hexaoxanonadecan-19-ol · ligand · chains A
- GOL · Glycerol · additive · 10 copies · chains A
- PGO · S-1,2-propanediol · additive · 2 copies · chains A
- BU1 · 1,4-butanediol · additive · chains A
- HEZ · Hexane-1,6-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1085 | 0.79 | 0.81 | 102 | ADP, GOL, P15 |
| 2 | 184 | 0.70 | 0.87 | 32 | empty |
| 3 | 444 | 0.67 | 0.79 | 47 | GOL |
| 4 | 105 | 0.66 | 0.90 | 24 | GOL, PGO |
| 5 | 205 | 0.50 | 0.76 | 38 | empty |
Compared structures
- 6QDJ · Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin · the same entry in another collection · chain A against A, TM-score 1.00
- P02566 · AlphaFold monomer V2.0 prediction for myosin-4 (P02566) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 P02566
- Elsewhere: RCSB PDB 6QDJ · PDBe 6QDJ · UniProt P02566
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