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Crystal Structure of AnkB Ankyrin Repeats R13-24 in complex with autoinhibition segment AI-c
Analyse Crystal Structure of AnkB Ankyrin Repeats R13-24 in complex with autoinhibition… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y4F
- Type
- protein
- Length
- 828 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.953
- Source
- Homo sapiens
- Molecule
- Ankyrin-2
- UniProt
- Q01484
- Ligands
- CA
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · resolution 1.953 · 2 distinct chains · 48% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ankyrin-2 | protein | 415 | 48% helix, 0% strand | Q01484 |
| B | Ankyrin-2 | protein | 413 | 48% helix, 0% strand | Q01484 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.40 | 0.78 | 19 | empty |
| 2 | 73 | 0.36 | 0.77 | 18 | empty |
| 3 | 51 | 0.26 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 439 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5Y4F · Crystal structure of ankb ankyrin repeats R13-24 in complex with autoinhibition segment… · 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 Q01484
- Elsewhere: RCSB PDB 5Y4F · PDBe 5Y4F · UniProt Q01484
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