Research workbench
Crystal structure of myosin viia IQ5-sah in complex with apo-cam
Analyse Crystal structure of myosin viia IQ5-sah in complex with apo-cam in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WSU
- Type
- protein
- Length
- 455 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; Unconventional myosin-viia
- UniProt
- P62158, P97479
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 4 distinct chains · 74% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 140 | 60% helix, 9% strand | P62158 |
| C | Unconventional myosin-viia | protein | 90 | 96% helix, 0% strand | P97479 |
| B | Calmodulin | protein | 134 | 59% helix, 6% strand | P62158 |
| D | Unconventional myosin-viia | protein | 91 | 98% helix, 0% strand | P97479 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 320 | 0.66 | 0.81 | 41 | empty |
| 2 | 66 | 0.42 | 0.81 | 19 | empty |
| 3 | 94 | 0.40 | 0.77 | 24 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1386 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 1320 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 225 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5WSU · Crystal structure of Myosin VIIa IQ5-SAH in complex with apo-CaM · the same entry in another collection · chain A against A, TM-score 1.00
- P97479 · AlphaFold monomer V2.0 prediction for unconventional myosin-viia (P97479) · a predicted model of the same protein · chain C against A, TM-score 0.55
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 P62158
- Every structure of UniProt P97479
- Elsewhere: RCSB PDB 5WSU · PDBe 5WSU · UniProt P62158 · UniProt P97479
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