Research workbench
Local refinement of ankyrin-1 (N-terminal half), class 1 of erythrocyte ankyrin-1 complex
Analyse Local refinement of ankyrin-1 (N-terminal half), class 1 of erythrocyte… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V0M
- Type
- protein
- Length
- 483 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ankyrin-1; Band 3 anion transport protein
- UniProt
- P16157, P02730
- Pockets
- 3 · best druggability 0.53
Structure
electron microscopy · 2 distinct chains · 52% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ankyrin-1 | protein | 451 | 53% helix, 1% strand | P16157 |
| W | Band 3 anion transport protein | protein | 32 | 47% helix, 3% strand | P02730 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.53 | 0.80 | 31 | empty |
| 2 | 135 | 0.47 | 0.78 | 20 | empty |
| 3 | 60 | 0.33 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–W · 1489 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 7V0M · Local refinement of ankyrin-1 (N-terminal half), class 1 of erythrocyte ankyrin-1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- P16157 · AlphaFold monomer V2.0 prediction for ankyrin-1 (P16157) · a predicted model of the same protein · chain A against A, TM-score 0.69
- P02730 · AlphaFold monomer V2.0 prediction for band 3 anion transport protein (P02730) · a predicted model of the same protein · chain W against A, TM-score 0.40
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 P16157
- Every structure of UniProt P02730
- Elsewhere: RCSB PDB 7V0M · PDBe 7V0M · UniProt P16157 · UniProt P02730
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