Research workbench
Crystal structure of amino acids 1729-1786 of human beta cardiac myosin fused to GP7 as anti-parallel four-helix bundle
Analyse Crystal structure of amino acids 1729-1786 of human beta cardiac myosin fused… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WME
- Type
- protein
- Length
- 365 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid assembly scaffolding PROTEIN,MYOSIN-7
- UniProt
- P13848, P12883
Structure
x-ray diffraction · 4 distinct chains · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid assembly scaffolding PROTEIN,MYOSIN-7 | protein | 91 | 87% helix, 0% strand | P13848, P12883 |
| B | Capsid assembly scaffolding PROTEIN,MYOSIN-7 | protein | 92 | 87% helix, 0% strand | P13848, P12883 |
| C | Capsid assembly scaffolding PROTEIN,MYOSIN-7 | protein | 93 | 87% helix, 0% strand | P13848, P12883 |
| D | Capsid assembly scaffolding PROTEIN,MYOSIN-7 | protein | 89 | 88% helix, 0% strand | P13848, P12883 |
Interfaces
6 interfaces between chains.
- B–C · 1404 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 1399 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 1126 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 1070 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 1043 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5WME · Crystal Structure of Amino Acids 1729-1786 of Human Beta Cardiac Myosin Fused to Gp7 as… · the same entry in another collection · chain A against A, TM-score 1.00
- P12883 · AlphaFold monomer V2.0 prediction for myosin-7 (P12883) · a predicted model of the same protein · chain A against A, TM-score 0.71
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 P13848
- Every structure of UniProt P12883
- Elsewhere: RCSB PDB 5WME · PDBe 5WME · UniProt P13848 · UniProt P12883
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