Research workbench
Crystal structure of ankyrin B/NDEL1 complex
Analyse Crystal structure of ankyrin B/NDEL1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KZJ
- Type
- protein
- Length
- 150 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ankyrin-2; Nuclear distribution protein nude-like 1
- UniProt
- Q01484, Q9ERR1
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 3 distinct chains · 75% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ankyrin-2 | protein | 69 | 75% helix, 0% strand | Q01484 |
| B | Nuclear distribution protein nude-like 1 | protein | 39 | 69% helix, 3% strand | Q9ERR1 |
| C | Nuclear distribution protein nude-like 1 | protein | 42 | 79% helix, 2% strand | Q9ERR1 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.35 | 0.78 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1448 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 1124 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 531 Ų buried · 5 hydrogen bonds · protein-protein
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 Q01484
- Every structure of UniProt Q9ERR1
- Elsewhere: RCSB PDB 6KZJ · PDBe 6KZJ · UniProt Q01484 · UniProt Q9ERR1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.