Research workbench
Cytoplasmic dynein-1 motor domain AAA1, AAA2, and AAA3 subunits
Analyse Cytoplasmic dynein-1 motor domain AAA1, AAA2, and AAA3 subunits in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Z8H
- Type
- protein
- Length
- 1,083 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytoplasmic dynein 1 heavy chain 1
- UniProt
- Q14204
- Ligands
- ADP, ATP, ANP, MG
- Pockets
- 13 · best druggability 0.77
Structure
electron microscopy · 1 distinct chain · 49% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytoplasmic dynein 1 heavy chain 1 | protein | 1083 | 49% helix, 12% strand | Q14204 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 954 | 0.77 | 0.80 | 82 | ATP |
| 2 | 457 | 0.70 | 0.81 | 62 | ANP |
| 3 | 386 | 0.63 | 0.78 | 40 | empty |
| 4 | 269 | 0.57 | 0.77 | 32 | ADP |
| 5 | 94 | 0.50 | 0.82 | 26 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 7Z8H · Cytoplasmic dynein-1 motor domain AAA1, AAA2, and AAA3 subunits · the same entry in another collection · chain A against A, 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 Q14204
- Elsewhere: RCSB PDB 7Z8H · PDBe 7Z8H · UniProt Q14204
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