MolNFT v1 · #158314 · protein
Structure & function of a new aspartylglucosaminuria variant
6NQ6 · N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase: “Structure & function of a new aspartylglucosaminuria variant”. X-ray diffraction, 6 pockets (best druggability 0.54). MolNFT v1 #158314 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6NQ6
- Type
- protein
- Length
- 556 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
- EC
- 3.5.1.26
- UniProt
- A0A376EJJ1
- Pockets
- 6 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase (EC 3.5.1.26) | protein | 134 | 47% helix, 16% strand | A0A376EJJ1 |
| B, D | N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase (EC 3.5.1.26) | protein | 144 | 26% helix, 34% strand | A0A376EJJ1 |
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 | 70 | 0.54 | 0.87 | 16 | empty |
| 2 | 50 | 0.53 | 0.89 | 21 | empty |
| 3 | 137 | 0.44 | 0.77 | 26 | empty |
| 4 | 141 | 0.41 | 0.74 | 30 | empty |
| 5 | 141 | 0.40 | 0.74 | 18 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2708 Ų buried · 54 hydrogen bonds · protein-protein
- A–B · 2649 Ų buried · 53 hydrogen bonds · protein-protein
- B–D · 702 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 605 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 595 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6NQ6 · Structure & function of a new Aspartylglucosaminuria variant · 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 A0A376EJJ1
- Elsewhere: RCSB PDB 6NQ6 · PDBe 6NQ6 · UniProt A0A376EJJ1
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