Research workbench
Cryo-EM structure of the actomyosin-V complex in the post-rigor transition state (appnhp, central 1ER, class 5)
Analyse Cryo-EM structure of the actomyosin-V complex in the post-rigor transition… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PMI
- Type
- protein
- Length
- 1,265 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Unconventional myosin-va; Actin, alpha skeletal muscle; Phalloidin; Myosin light chain 6B
- UniProt
- Q02440, P68135, P14649
- Ligands
- ANP, ADP, MG
- Pockets
- 18 · best druggability 0.78
Structure
electron microscopy · 4 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Unconventional myosin-va | protein | 747 | 47% helix, 16% strand | Q02440 |
| C | Actin, alpha skeletal muscle | protein | 372 | 43% helix, 20% strand | P68135 |
| H | Phalloidin | protein | 7 | 0% helix, 0% strand | — |
| B | Myosin light chain 6B | protein | 139 | 61% helix, 7% strand | P14649 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains C
- MG · Magnesium ion · metal · 3 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1085 | 0.78 | 0.80 | 77 | empty |
| 2 | 401 | 0.74 | 0.85 | 52 | ADP, MG |
| 3 | 627 | 0.72 | 0.79 | 60 | empty |
| 4 | 304 | 0.62 | 0.79 | 41 | empty |
| 5 | 108 | 0.60 | 0.87 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1474 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 958 Ų buried · 12 hydrogen bonds · protein-protein
- C–H · 214 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified, 1 d-amino (D-amino acid, hydroxylation, methylation, nonstandard).
Compared structures
- 7PMI · Cryo-EM structure of the actomyosin-V complex in the post-rigor transition state (AppNHp… · the same entry in another collection · chain A against A, TM-score 1.00
- P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain C against A, TM-score 0.96
- P14649 · AlphaFold monomer V2.0 prediction for myosin light chain 6B (P14649) · a predicted model of the same protein · chain B against A, TM-score 0.95
- Q02440 · AlphaFold monomer V2.0 prediction for unconventional myosin-va (Q02440) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q02440
- Every structure of UniProt P68135
- Every structure of UniProt P14649
- Elsewhere: RCSB PDB 7PMI · PDBe 7PMI · UniProt Q02440 · UniProt P68135 · UniProt P14649
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