Research workbench
Filamentous actin decorated with human cardiac myosin binding protein C C2 domain
Analyse Filamentous actin decorated with human cardiac myosin binding protein C C2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LRG
- Type
- protein
- Length
- 2,790 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha cardiac muscle 1; Myosin-binding protein C, cardiac-type
- UniProt
- B6VNT8, Q14896
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 2 distinct chains · 30% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Actin, alpha cardiac muscle 1 | protein | 371 | 38% helix, 16% strand | B6VNT8 |
| G, H, I, J, K, L | Myosin-binding protein C, cardiac-type | protein | 94 | 0% helix, 53% strand | Q14896 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 836 | 0.81 | 0.84 | 96 | empty |
| 2 | 651 | 0.78 | 0.83 | 68 | empty |
| 3 | 185 | 0.75 | 0.91 | 36 | empty |
| 4 | 190 | 0.75 | 0.91 | 34 | empty |
| 5 | 187 | 0.74 | 0.91 | 35 | empty |
Interfaces
19 interfaces between chains.
- D–F · 1242 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 1241 Ų buried · 12 hydrogen bonds · protein-protein
- C–E · 1239 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 1237 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 449 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7LRG · Filamentous actin decorated with human cardiac myosin binding protein C C2 domain · the same entry in another collection · chain L against L, TM-score 1.00
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 B6VNT8
- Every structure of UniProt Q14896
- Elsewhere: RCSB PDB 7LRG · PDBe 7LRG · UniProt B6VNT8 · UniProt Q14896
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