Research workbench
Outer dynein arm-shulin complex - DYH3 motor region (tetrahymena thermophila)
Analyse Outer dynein arm-shulin complex - DYH3 motor region (tetrahymena thermophila) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZYY
- Type
- protein
- Length
- 2,967 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dynein heavy chain, outer arm protein; Shulin
- UniProt
- Q22A67, Q22YU3
- Ligands
- ADP, ATP
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 2 distinct chains · 51% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Dynein heavy chain, outer arm protein | protein | 2901 | 51% helix, 8% strand | Q22A67 |
| Y | Shulin | protein | 66 | 39% helix, 3% strand | Q22YU3 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains C
- ATP · Adenosine-5'-triphosphate · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1189 | 0.86 | 0.87 | 118 | ADP |
| 2 | 1080 | 0.84 | 0.85 | 127 | empty |
| 3 | 610 | 0.81 | 0.87 | 64 | ADP |
| 4 | 904 | 0.80 | 0.82 | 106 | ADP |
| 5 | 1022 | 0.80 | 0.81 | 91 | empty |
Interfaces
1 interface between chains.
- C–Y · 745 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6ZYY · Outer Dynein Arm-Shulin complex - Dyh3 motor region (Tetrahymena thermophila) · the same entry in another collection · chain C against C, 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 Q22A67
- Every structure of UniProt Q22YU3
- Elsewhere: RCSB PDB 6ZYY · PDBe 6ZYY · UniProt Q22A67 · UniProt Q22YU3
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