Research workbench
Complex structure of C-terminal cftr peptide and extended PDZ1 domain from NHERF1
Analyse Complex structure of C-terminal cftr peptide and extended PDZ1 domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M0U
- Type
- protein
- Length
- 122 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O14745
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 117 | — | O14745 |
| B | — | protein | 5 | — | — |
Compared structures
- 2M0U · Complex structure of C-terminal CFTR peptide and extended PDZ1 domain from NHERF1 · the same entry in another collection · chain A against A, TM-score 1.00
- O14745 · AlphaFold monomer V2.0 prediction for NA(+)/H(+) exchange regulatory cofactor nhe-RF1… · a predicted model of the same protein · chain A against A, TM-score 0.80
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 O14745
- Elsewhere: RCSB PDB 2M0U · PDBe 2M0U · UniProt O14745
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