Research workbench
Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
Analyse Molecular models of averaged rigor crossbridges from tomograms of insect flight… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O1E
- Type
- protein
- Length
- 12,000 residues
- Chains
- 32
- 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 0.82
Structure
electron microscopy · 4 distinct chains · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J, M, P | Skeletal muscle myosin II | protein | 840 | 47% helix, 13% strand | P13538 |
| B, E, H, K, N, Q | Skeletal muscle myosin II regulatory light chain | protein | 145 | 58% helix, 3% strand | P02609 |
| C, F, I, L, O, R | Skeletal muscle myosin II essential light chain | protein | 147 | 56% helix, 5% strand | P02605 |
| 1, 2, 3, 4, 5, 6, 7, 8, 9, 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 | 1057 | 0.82 | 0.83 | 106 | empty |
| 2 | 1088 | 0.82 | 0.83 | 108 | empty |
| 3 | 1076 | 0.82 | 0.83 | 104 | empty |
| 4 | 1008 | 0.82 | 0.83 | 106 | empty |
| 5 | 1036 | 0.82 | 0.83 | 110 | empty |
Interfaces
60 interfaces between chains.
- G–H · 1735 Ų buried · 23 hydrogen bonds · protein-protein
- J–K · 1642 Ų buried · 21 hydrogen bonds · protein-protein
- M–N · 1624 Ų buried · 21 hydrogen bonds · protein-protein
- P–Q · 1603 Ų buried · 22 hydrogen bonds · protein-protein
- P–R · 1588 Ų buried · 38 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 270 modified, 15 isopeptide (methylation, isopeptide).
Compared structures
- 1O1E · 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 1O1E · PDBe 1O1E · UniProt P13538 · UniProt P02609 · UniProt P02605 · UniProt P68135
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