Research workbench
Cryo-EM structure of human ATG9A in lmng micelles
Analyse Cryo-EM structure of human ATG9A in lmng micelles in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JLQ
- Type
- protein
- Length
- 1,422 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Autophagy-related protein 9A
- UniProt
- Q7Z3C6
- Pockets
- 20 · best druggability 0.76
Structure
electron microscopy · 1 distinct chain · 65% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Autophagy-related protein 9A | protein | 474 | 65% helix, 5% strand | Q7Z3C6 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 651 | 0.76 | 0.81 | 80 | empty |
| 2 | 716 | 0.74 | 0.80 | 72 | empty |
| 3 | 348 | 0.69 | 0.82 | 38 | empty |
| 4 | 449 | 0.69 | 0.80 | 37 | empty |
| 5 | 434 | 0.68 | 0.80 | 37 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1668 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 1658 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 1641 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 Q7Z3C6
- Elsewhere: RCSB PDB 7JLQ · PDBe 7JLQ · UniProt Q7Z3C6
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