Research workbench
Aspartylglucosaminuria mutant structure and function
Analyse Aspartylglucosaminuria mutant structure and function in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DEY
- Type
- protein
- Length
- 566 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosylasparaginase, residues 38-178; Glycosylasparaginase, residues 188-331
- UniProt
- A0A1V3U2Z4
- Pockets
- 6 · best druggability 0.51
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosylasparaginase, residues 38-178 | protein | 141 | 44% helix, 16% strand | A0A1V3U2Z4 |
| B, D | Glycosylasparaginase, residues 188-331 | protein | 144 | 26% helix, 35% strand | A0A1V3U2Z4 |
| C | Glycosylasparaginase, residues 38-178 | protein | 137 | 44% helix, 15% strand | A0A1V3U2Z4 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.51 | 0.84 | 16 | empty |
| 2 | 63 | 0.50 | 0.86 | 25 | empty |
| 3 | 68 | 0.47 | 0.83 | 17 | empty |
| 4 | 151 | 0.45 | 0.76 | 24 | empty |
| 5 | 132 | 0.44 | 0.77 | 23 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2682 Ų buried · 51 hydrogen bonds · protein-protein
- C–D · 2673 Ų buried · 51 hydrogen bonds · protein-protein
- A–D · 704 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 701 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 698 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6DEY · Aspartylglucosaminuria mutant structure and function · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A1V3U2Z4
- Elsewhere: RCSB PDB 6DEY · PDBe 6DEY · UniProt A0A1V3U2Z4
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