Research workbench
Structural studies on the effects of the deletion in the red cell anion exchanger (BAND3, AE1) associated with south east asian ovalocytosis.
Analyse Structural studies on the effects of the deletion in the red cell anion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BNX
- Type
- protein
- Length
- 33 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (band 3)
- UniProt
- P02730
- Ligands
- ACE
Structure
solution nmr · 1 distinct chain · 58% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (band 3) | protein | 33 | 58% helix, 0% strand | P02730 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1BNX · Structural studies on the effects of the deletion in the red cell anion exchanger (BAND3… · the same entry in another collection · chain A against A, TM-score 1.00
- P02730 · AlphaFold monomer V2.0 prediction for band 3 anion transport protein (P02730) · a predicted model of the same protein · chain A against A, TM-score 0.61
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
- Elsewhere: RCSB PDB 1BNX · PDBe 1BNX · UniProt P02730
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