Research workbench
Cryo-EM structure of human band 3-protein 4.2 complex in vertical conformation
Analyse Cryo-EM structure of human band 3-protein 4.2 complex in vertical conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TW0
- Type
- protein
- Length
- 2,309 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Band 3 anion transport protein; Protein 4.2
- UniProt
- P02730, P16452
- Ligands
- NAG
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 3 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Band 3 anion transport protein | protein | 814 | 54% helix, 11% strand | P02730 |
| A | Band 3 anion transport protein | protein | 830 | 53% helix, 10% strand | P02730 |
| E | Protein 4.2 | protein | 665 | 16% helix, 39% strand | P16452 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 814 | 0.87 | 0.90 | 77 | empty |
| 2 | 793 | 0.80 | 0.83 | 77 | empty |
| 3 | 638 | 0.79 | 0.84 | 62 | empty |
| 4 | 107 | 0.77 | 0.97 | 31 | empty |
| 5 | 742 | 0.77 | 0.82 | 79 | empty |
Interfaces
2 interfaces between chains.
- B–A · 3932 Ų buried · 32 hydrogen bonds · protein-protein
- A–E · 1907 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 glycan (N-glycosylation).
Compared structures
- 7TW0 · Cryo-EM structure of human band 3-protein 4.2 complex in vertical conformation · the same entry in another collection · chain B against B, 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
- 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
- Elsewhere: RCSB PDB 7TW0 · PDBe 7TW0 · UniProt P02730 · UniProt P16452
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