Research workbench
Solution structure of the N-terminal domain of pig gastric H/K-ATPase
Analyse Solution structure of the N-terminal domain of pig gastric H/K-ATPase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IWF
- Type
- protein
- Length
- 34 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gastric H/K-ATPase
- EC
- 3.6.3.10
- UniProt
- P19156
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gastric H/K-ATPase (EC 3.6.3.10) | protein | 34 | 0% helix, 0% strand | P19156 |
Compared structures
- 1IWF · Solution structure of the N-terminal domain of pig gastric H/K-ATPase · the same entry in another collection · chain A against A, TM-score 1.00
- P19156 · AlphaFold monomer V2.0 prediction for potassium-transporting ATPase alpha chain 1 (P19156) · a predicted model of the same protein · chain A against A, TM-score 0.31
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 P19156
- Elsewhere: RCSB PDB 1IWF · PDBe 1IWF · UniProt P19156
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