Research workbench
Crystal structure of arabidopsis thaliana dj-1D
Analyse Crystal structure of arabidopsis thaliana dj-1D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UK7
- Type
- protein
- Length
- 1,168 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Class I glutamine amidotransferase-like domain-containing protein
- UniProt
- Q9M8R4
- Pockets
- 14 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Class I glutamine amidotransferase-like domain-containing protein | protein | 386 | 35% helix, 25% strand | Q9M8R4 |
| C | Class I glutamine amidotransferase-like domain-containing protein | protein | 396 | 34% helix, 24% strand | Q9M8R4 |
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.72 | 0.98 | 23 | empty |
| 2 | 117 | 0.71 | 0.92 | 33 | empty |
| 3 | 120 | 0.70 | 0.92 | 28 | empty |
| 4 | 391 | 0.61 | 0.77 | 44 | empty |
| 5 | 530 | 0.59 | 0.73 | 52 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1250 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1237 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 1236 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 modified (engineered, oxidation).
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 Q9M8R4
- Elsewhere: RCSB PDB 3UK7 · PDBe 3UK7 · UniProt Q9M8R4
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