MolNFT v1 · #43923 · protein
1H chemical shift assignments for the secondary transmembrane domain from human copper transport 1
2LS3: “1H chemical shift assignments for the secondary transmembrane domain from human copper transport 1”. Solution nmr. MolNFT v1 #43923 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2LS3
- Type
- protein
- Length
- 29 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O15431
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 29 | — | O15431 |
Compared structures
- 2LS3 · 1H Chemical Shift Assignments for the secondary transmembrane domain from 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 0.54
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 2LS3 · PDBe 2LS3 · UniProt O15431
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