MolNFT v1 · #2540 · protein
Structural studies on the effects of the deletion in the red cell anion exchanger (BAND3, AE1) associated with south east asian ovalocytosis.
1BZK · Protein (band 3 anion transport protein): “Structural studies on the effects of the deletion in the red cell anion exchanger (BAND3, AE1) associated…”. Solution nmr, 1 ligand (ACE). MolNFT v1 #2540 on GenesisL1: 3D structure…
- PDB
- 1BZK
- Type
- protein
- Length
- 42 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (band 3 anion transport protein)
- UniProt
- P02730
- Ligands
- ACE
Structure
solution nmr · 1 distinct chain · 38% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (band 3 anion transport protein) | protein | 42 | 38% 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
- 1BZK · 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 0.44
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 1BZK · PDBe 1BZK · UniProt P02730
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