MolNFT v1 · #14840 · protein
X-ray structures of the mgadp, mgatpgammas, and mgamppnp complexes of the dictyostelium discoideum myosin motor domain
1MMA: “X-ray structures of the mgadp, mgatpgammas, and mgamppnp complexes of the dictyostelium discoideum myosin…”. X-ray diffraction, 2 ligands (ADP, MG), 7 pockets (best druggability 0.85). MolNFT v1 #14840 on GenesisL1: 3D structure…
- PDB
- 1MMA
- Type
- protein
- Length
- 719 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin
- EC
- 3.6.1.32
- UniProt
- P08799
- Ligands
- ADP, MG
- Pockets
- 7 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin (EC 3.6.1.32) | protein | 719 | 45% helix, 14% strand | P08799 |
Ligands and binding sites
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 | 1106 | 0.85 | 0.86 | 126 | MG, ADP |
| 2 | 362 | 0.63 | 0.78 | 42 | empty |
| 3 | 263 | 0.61 | 0.80 | 47 | empty |
| 4 | 109 | 0.43 | 0.78 | 22 | empty |
| 5 | 101 | 0.36 | 0.75 | 21 | empty |
Compared structures
- 1MMA · X-ray structures of the mgadp, mgatpgammas, and mgamppnp complexes of the dictyostelium… · the same entry in another collection · chain A against A, TM-score 1.00
- P08799 · AlphaFold monomer V2.0 prediction for myosin-2 heavy chain (P08799) · 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 P08799
- Elsewhere: RCSB PDB 1MMA · PDBe 1MMA · UniProt P08799
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