Research workbench
1H chemical shift assignments for the third transmembrane domain from the human copper transport 1
Analyse 1H chemical shift assignments for the third transmembrane domain from the human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LS4
- Type
- protein
- Length
- 24 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High affinity copper uptake protein 1
- UniProt
- O15431
Structure
solution nmr · 1 distinct chain · 42% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High affinity copper uptake protein 1 | protein | 24 | 42% helix, 0% strand | O15431 |
Compared structures
- 2LS4 · 1H Chemical Shift Assignments for the third transmembrane domain from the human copper… · the same entry in another collection · chain A against A, TM-score 1.00
- O15431 · AlphaFold monomer V2.0 prediction for high affinity copper uptake protein 1 (O15431) · a predicted model of the same protein · chain A against A, TM-score 0.29
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 O15431
- Elsewhere: RCSB PDB 2LS4 · PDBe 2LS4 · UniProt O15431
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