Research workbench
Structural and functional analysis of tm XI of the NHE1 isoform of the NA+/H+ exchanger
Analyse Structural and functional analysis of tm XI of the NHE1 isoform of the NA+/H+… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KBV
- Type
- protein
- Length
- 26 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SODIUM/HYDROGEN exchanger 1
- UniProt
- P19634
- Ligands
- ACE, NH2
Structure
solution nmr · 1 distinct chain · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SODIUM/HYDROGEN exchanger 1 | protein | 26 | 81% helix, 0% strand | P19634 |
Ligands and binding sites
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
- 2KBV · Structural and functional analysis of TM XI of the NHE1 isoform of thE NA+/H+ exchanger · the same entry in another collection · chain A against A, TM-score 1.00
- P19634 · AlphaFold monomer V2.0 prediction for SODIUM/HYDROGEN exchanger 1 (P19634) · a predicted model of the same protein · chain A against A, TM-score 0.37
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 P19634
- Elsewhere: RCSB PDB 2KBV · PDBe 2KBV · UniProt P19634
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