MolNFT v1 · #158696 · protein
The N-terminal domain of NPHP1 folds into an antiparallel three- stranded coiled coil
6O1Q · Nephrocystin-1: “The N-terminal domain of NPHP1 folds into an antiparallel three- stranded coiled coil”. Solution nmr. MolNFT v1 #158696 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6O1Q
- Type
- protein
- Length
- 119 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nephrocystin-1
- UniProt
- O15259
Structure
solution nmr · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nephrocystin-1 | protein | 119 | 68% helix, 0% strand | O15259 |
Compared structures
- 6O1Q · The N-terminal domain of NPHP1 folds into an antiparallel three-stranded coiled coil · the same entry in another collection · chain A against A, TM-score 1.00
- O15259 · AlphaFold monomer V2.0 prediction for nephrocystin-1 (O15259) · a predicted model of the same protein · chain A against A, TM-score 0.79
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 O15259
- Elsewhere: RCSB PDB 6O1Q · PDBe 6O1Q · UniProt O15259
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