MolNFT v1 · #160276 · protein
Crystal structure of amino acids 1473-1536 of human beta cardiac myosin fused to GP7 and EB1
6PFP · Myosin-7 fused to GP7 and EB1: “Crystal structure of amino acids 1473-1536 of human beta cardiac myosin fused to GP7 and EB1”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.61). MolNFT v1 #160276 on GenesisL1: 3D…
- PDB
- 6PFP
- Type
- protein
- Length
- 624 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin-7 fused to GP7 and EB1
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 90% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin-7 fused to GP7 and EB1 | protein | 156 | 89% helix, 0% strand | — |
| B, C, D | Myosin-7 fused to GP7 and EB1 | protein | 156 | 90% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 8 copies · chains A, B, D, C
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 | 296 | 0.61 | 0.79 | 42 | MPD |
| 2 | 83 | 0.38 | 0.76 | 10 | MPD |
Interfaces
5 interfaces between chains.
- A–B · 4223 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 4175 Ų buried · 28 hydrogen bonds · protein-protein
- A–D · 571 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 371 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 175 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6PFP · Crystal Structure of Amino Acids 1473-1536 of Human Beta Cardiac Myosin Fused to Gp7 and… · 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
- Elsewhere: RCSB PDB 6PFP · PDBe 6PFP
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