MolNFT v1 · #126341 · protein
Chicken smooth muscle myosin motor domain co-crystallized with the specific ck-571 inhibitor, mgadp form
5M05 · Myosin-11: “Chicken smooth muscle myosin motor domain co-crystallized with the specific ck-571 inhibitor, mgadp form”. X-ray diffraction, 3 ligands (52E, ADP, MG), 7 pockets (best druggability 0.78). MolNFT v1 #126341 on GenesisL1…
- PDB
- 5M05
- Type
- protein
- Length
- 707 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin-11
- UniProt
- P10587
- Ligands
- 52E, ADP, MG
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin-11 | protein | 707 | 45% helix, 16% strand | P10587 |
Ligands and binding sites
- 52E · 4-{[(2-chloro-3-fluorobenzyl)carbamoyl](methyl)amino}-3,4-dideoxy-5-O-(isoquinolin-3-ylcarbamoyl)-D-erythro-pentitol · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1117 | 0.78 | 0.80 | 106 | ADP |
| 2 | 425 | 0.75 | 0.84 | 53 | 52E |
| 3 | 97 | 0.75 | 0.96 | 21 | empty |
| 4 | 152 | 0.45 | 0.76 | 18 | empty |
| 5 | 60 | 0.34 | 0.77 | 11 | empty |
Compared structures
- 5M05 · Chicken smooth muscle myosin motor domain co-crystallized with the specific CK-571… · the same entry in another collection · chain A against A, TM-score 1.00
- P10587 · AlphaFold monomer V2.0 prediction for myosin-11 (P10587) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P10587
- Elsewhere: RCSB PDB 5M05 · PDBe 5M05 · UniProt P10587
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