Research workbench
Structure of the full-length yeast ARP7-ARP9 heterodimer
Analyse Structure of the full-length yeast ARP7-ARP9 heterodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WEE
- Type
- protein
- Length
- 840 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin-like protein ARP9; Actin-related protein 7
- UniProt
- Q05123, Q12406
- Ligands
- SO4
- Pockets
- 12 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin-like protein ARP9 | protein | 428 | 37% helix, 19% strand | Q05123 |
| B | Actin-related protein 7 | protein | 412 | 47% helix, 18% strand | Q12406 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1019 | 0.85 | 0.86 | 114 | CXS, SO4 |
| 2 | 147 | 0.79 | 0.96 | 37 | SO4 |
| 3 | 432 | 0.68 | 0.80 | 60 | SO4 |
| 4 | 158 | 0.53 | 0.80 | 24 | empty |
| 5 | 134 | 0.48 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1632 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (nonstandard).
Compared structures
- 3WEE · Structure of the full-length yeast Arp7-Arp9 Heterodimer · the same entry in another collection · chain A against A, TM-score 1.00
- Q05123 · AlphaFold monomer V2.0 prediction for actin-like protein ARP9 (Q05123) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q12406 · AlphaFold monomer V2.0 prediction for actin-related protein 7 (Q12406) · a predicted model of the same protein · chain B against A, TM-score 0.92
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 Q05123
- Every structure of UniProt Q12406
- Elsewhere: RCSB PDB 3WEE · PDBe 3WEE · UniProt Q05123 · UniProt Q12406
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