Research workbench
Cryo-EM structure of the actomyosin-V complex in the rigor state (central 3ER/2ER)
Analyse Cryo-EM structure of the actomyosin-V complex in the rigor state (central… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PLU
- Type
- protein
- Length
- 2,909 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q02440, P68135, P14649
- Ligands
- ADP, MG
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 747 | — | Q02440 |
| C, F, G | — | protein | 372 | — | P68135 |
| H, I, J | — | protein | 7 | — | — |
| B, E | — | protein | 139 | — | P14649 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains C, F, G
- MG · Magnesium ion · metal · 3 copies · chains C, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7PLU · Cryo-EM structure of the actomyosin-V complex in the rigor state (central 3er/2er) · the same entry in another collection · chain J against J, TM-score 1.00
- P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain G against A, TM-score 0.96
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 7PLU · PDBe 7PLU · UniProt Q02440 · UniProt P68135 · UniProt P14649
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