MolNFT v1 · #16517 · protein
Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1F · Skeletal muscle myosin II: “Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle”. Electron microscopy, 20 pockets (best druggability 0.83). MolNFT v1 #16517 on GenesisL1: 3D structure, binding…
- PDB
- 1O1F
- Type
- protein
- Length
- 9,736 residues
- Chains
- 26
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Skeletal muscle myosin II; Skeletal muscle myosin II regulatory light chain; Skeletal…
- UniProt
- P13538, P02609, P02605, P68135
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 4 distinct chains · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | Skeletal muscle myosin II | protein | 840 | 47% helix, 13% strand | P13538 |
| B, E, H, K | Skeletal muscle myosin II regulatory light chain | protein | 145 | 58% helix, 3% strand | P02609 |
| C, F, I, L | Skeletal muscle myosin II essential light chain | protein | 147 | 56% helix, 5% strand | P02605 |
| 0, 1, 2, 3, 4, 5, 6, 7, 8, V, W, X, Y, Z | Skeletal muscle actin | protein | 372 | 42% helix, 20% strand | P68135 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1103 | 0.83 | 0.84 | 94 | empty |
| 2 | 1043 | 0.82 | 0.83 | 103 | empty |
| 3 | 1091 | 0.82 | 0.83 | 113 | empty |
| 4 | 1054 | 0.82 | 0.83 | 107 | empty |
| 5 | 1079 | 0.82 | 0.83 | 114 | empty |
Interfaces
46 interfaces between chains.
- G–H · 1616 Ų buried · 21 hydrogen bonds · protein-protein
- J–K · 1532 Ų buried · 20 hydrogen bonds · protein-protein
- G–6 · 1513 Ų buried · 104 hydrogen bonds · protein-protein
- D–5 · 1511 Ų buried · 104 hydrogen bonds · protein-protein
- J–7 · 1507 Ų buried · 105 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 180 modified, 10 isopeptide (methylation, isopeptide).
Compared structures
- 1O1F · Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle · the same entry in another collection · chain H against H, 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 P13538
- Every structure of UniProt P02609
- Every structure of UniProt P02605
- Every structure of UniProt P68135
- Elsewhere: RCSB PDB 1O1F · PDBe 1O1F · UniProt P13538 · UniProt P02609 · UniProt P02605 · UniProt P68135
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