Research workbench
Solution structure of the N-terminal domain of a potential copper- translocating P-type ATPase from bacillus subtilis in the CU(I)LOADED state
Analyse Solution structure of the N-terminal domain of a potential copper… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KQK
- Type
- protein
- Length
- 80 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O32220
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 80 | — | O32220 |
Compared structures
- 1KQK · Solution Structure of the N-terminal Domain of a Potential Copper-translocating P-type… · the same entry in another collection · chain A against A, TM-score 1.00
- O32220 · AlphaFold monomer V2.0 prediction for copper-exporting P-type ATPase (O32220) · a predicted model of the same protein · chain A against A, TM-score 0.85
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 O32220
- Elsewhere: RCSB PDB 1KQK · PDBe 1KQK · UniProt O32220
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