Research workbench
X-ray structures of the mgadp, mgatpgammas, and mgamppnp complexes of the dictyostelium discoideum myosin motor domain
Analyse X-ray structures of the mgadp, mgatpgammas, and mgamppnp complexes of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MMN
- Type
- protein
- Length
- 737 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
- ANP, MG
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin (EC 3.6.1.32) | protein | 737 | 47% helix, 15% strand | P08799 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · 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
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 955 | 0.84 | 0.86 | 111 | MG, ANP |
| 2 | 953 | 0.72 | 0.76 | 76 | empty |
| 3 | 78 | 0.66 | 0.92 | 22 | empty |
| 4 | 106 | 0.50 | 0.81 | 20 | empty |
| 5 | 65 | 0.38 | 0.79 | 16 | empty |
Compared structures
- 1MMN · 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 0.89
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 1MMN · PDBe 1MMN · UniProt P08799
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