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Crystal structure of autophagic E2, ATG10
Analyse Crystal structure of autophagic E2, ATG10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EBR
- Type
- protein
- Length
- 314 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-like-conjugating enzyme ATG10
- EC
- 6.3.2.-
- UniProt
- Q07879
- Ligands
- HG
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ubiquitin-like-conjugating enzyme ATG10 (EC 6.3.2.-) | protein | 157 | 26% helix, 34% strand | Q07879 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 217 | 0.64 | 0.83 | 46 | empty |
| 2 | 76 | 0.55 | 0.87 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 964 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 Q07879
- Elsewhere: RCSB PDB 4EBR · PDBe 4EBR · UniProt Q07879
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