Research workbench
Crystal structure of rigor-like human nonmuscle myosin-2B
Analyse Crystal structure of rigor-like human nonmuscle myosin-2B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PD3
- Type
- protein
- Length
- 1,852 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nonmuscle myosin heavy chain B, alpha-actinin a chimera protein
- UniProt
- P35580, P05095
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nonmuscle myosin heavy chain B, alpha-actinin a chimera protein | protein | 922 | 52% helix, 12% strand | P35580, P05095 |
| B | Nonmuscle myosin heavy chain B, alpha-actinin a chimera protein | protein | 930 | 54% helix, 10% strand | P35580, P05095 |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1097 | 0.75 | 0.78 | 78 | empty |
| 2 | 702 | 0.73 | 0.79 | 58 | empty |
| 3 | 515 | 0.72 | 0.81 | 61 | empty |
| 4 | 366 | 0.71 | 0.83 | 40 | empty |
| 5 | 336 | 0.70 | 0.83 | 43 | empty |
Interfaces
1 interface between chains.
- A–B · 1454 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 4PD3 · Crystal Structure of Rigor-Like Human Nonmuscle Myosin-2B · the same entry in another collection · chain A against A, TM-score 1.00
- P35580 · AlphaFold monomer V2.0 prediction for myosin-10 (P35580) · a predicted model of the same protein · chain A against A, TM-score 0.66
- P05095 · AlphaFold monomer V2.0 prediction for alpha-actinin a (P05095) · a predicted model of the same protein · chain B against A, TM-score 0.31
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 P35580
- Every structure of UniProt P05095
- Elsewhere: RCSB PDB 4PD3 · PDBe 4PD3 · UniProt P35580 · UniProt P05095
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