Research workbench
A PIP2 and F-actin-binding site of gelsolin, residue 150-169 (NMR, averaged structure)
Analyse A PIP2 and F-actin-binding site of gelsolin, residue 150-169 (NMR, averaged… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SOL
- Type
- protein
- Length
- 20 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Molecule
- Gelsolin (150-169)
- UniProt
- P06396
Structure
solution nmr · resolution NOT · 1 distinct chain · 40% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gelsolin (150-169) | protein | 20 | 40% helix, 0% strand | P06396 |
Compared structures
- 1SOL · A PIP2 and F-actin-binding site of gelsolin, residue 150-169 (NMR, averaged structure) · the same entry in another collection · chain A against A, TM-score 1.00
- P06396 · AlphaFold monomer V2.0 prediction for gelsolin (P06396) · a predicted model of the same protein · chain A against A, TM-score 0.42
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 P06396
- Elsewhere: RCSB PDB 1SOL · PDBe 1SOL · UniProt P06396
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