Research workbench
Cryo-EM structure of human ankyrin complex (B2P1A2) from red blood cell
Analyse Cryo-EM structure of human ankyrin complex (B2P1A2) from red blood cell in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TW5
- Type
- protein
- Length
- 3,579 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Band 3 anion transport protein; Protein 4.2; Ankyrin-1
- UniProt
- P02730, P16452, P16157
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 4 distinct chains · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Band 3 anion transport protein | protein | 830 | 54% helix, 10% strand | P02730 |
| B | Band 3 anion transport protein | protein | 814 | 53% helix, 11% strand | P02730 |
| E | Protein 4.2 | protein | 665 | 17% helix, 38% strand | P16452 |
| G, H | Ankyrin-1 | protein | 635 | 48% helix, 0% strand | P16157 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 717 | 0.87 | 0.91 | 104 | empty |
| 2 | 849 | 0.83 | 0.85 | 96 | empty |
| 3 | 457 | 0.81 | 0.89 | 68 | empty |
| 4 | 151 | 0.80 | 0.96 | 28 | empty |
| 5 | 775 | 0.79 | 0.82 | 70 | empty |
Interfaces
4 interfaces between chains.
- A–B · 3735 Ų buried · 30 hydrogen bonds · protein-protein
- A–E · 1607 Ų buried · 22 hydrogen bonds · protein-protein
- E–G · 1178 Ų buried · 12 hydrogen bonds · protein-protein
- B–H · 620 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7TW5 · Cryo-EM structure of human ankyrin complex (B2P1A2) from red blood cell · the same entry in another collection · chain H against H, TM-score 1.00
- P16452 · AlphaFold monomer V2.0 prediction for protein 4.2 (P16452) · a predicted model of the same protein · chain E against A, TM-score 0.96
- P16157 · AlphaFold monomer V2.0 prediction for ankyrin-1 (P16157) · a predicted model of the same protein · chain H against A, TM-score 0.89
- P02730 · AlphaFold monomer V2.0 prediction for band 3 anion transport protein (P02730) · a predicted model of the same protein · chain B against A, TM-score 0.65
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 P02730
- Every structure of UniProt P16452
- Every structure of UniProt P16157
- Elsewhere: RCSB PDB 7TW5 · PDBe 7TW5 · UniProt P02730 · UniProt P16452 · UniProt P16157
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