Research workbench
Crystal structure of alpha-cop-WD40 domain, Y139A mutant
Analyse Crystal structure of alpha-cop-WD40 domain, Y139A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S23
- Type
- protein
- Length
- 923 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coatomer subunit alpha
- UniProt
- Q96WV5
- Ligands
- ACE
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 2% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coatomer subunit alpha | protein | 307 | 2% helix, 56% strand | Q96WV5 |
| B | Coatomer subunit alpha | protein | 312 | 3% helix, 55% strand | Q96WV5 |
| C | Coatomer subunit alpha | protein | 304 | 2% helix, 56% strand | Q96WV5 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 764 | 0.82 | 0.85 | 52 | empty |
| 2 | 753 | 0.82 | 0.85 | 53 | empty |
| 3 | 640 | 0.81 | 0.85 | 43 | empty |
| 4 | 1064 | 0.70 | 0.75 | 116 | empty |
| 5 | 131 | 0.58 | 0.84 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–C · 565 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 531 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 278 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (covalent ligand).
Compared structures
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 Q96WV5
- Elsewhere: RCSB PDB 7S23 · PDBe 7S23 · UniProt Q96WV5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.