Research workbench
Crystal structure of the N-terminal domain of ATG2
Analyse Crystal structure of the N-terminal domain of ATG2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A9E
- Type
- protein
- Length
- 678 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ENDOLYSIN,AUTOPHAGY-related protein 2
- EC
- 3.2.1.17
- UniProt
- A0A097J809, O94649
- Pockets
- 10 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ENDOLYSIN,AUTOPHAGY-related protein 2 (EC 3.2.1.17) | protein | 339 | 53% helix, 22% strand | A0A097J809, O94649 |
| B | ENDOLYSIN,AUTOPHAGY-related protein 2 (EC 3.2.1.17) | protein | 339 | 51% helix, 24% strand | A0A097J809, O94649 |
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.83 | 0.93 | 29 | empty |
| 2 | 1126 | 0.82 | 0.84 | 110 | empty |
| 3 | 517 | 0.76 | 0.82 | 40 | empty |
| 4 | 491 | 0.75 | 0.82 | 36 | empty |
| 5 | 330 | 0.66 | 0.81 | 44 | empty |
Interfaces
1 interface between chains.
- A–B · 1647 Ų buried · 32 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 21 modified (engineered).
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 A0A097J809
- Every structure of UniProt O94649
- Elsewhere: RCSB PDB 6A9E · PDBe 6A9E · UniProt A0A097J809 · UniProt O94649
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