Research workbench
Structural basis for Ca2+-mediated interaction of the perforin C2 domain with lipid membranes
Analyse Structural basis for Ca2+-mediated interaction of the perforin C2 domain with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Y1S
- Type
- protein
- Length
- 122 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.611
- Source
- Mus musculus
- Molecule
- Perforin-1
- UniProt
- P10820
- Ligands
- CA
Structure
x-ray diffraction · resolution 1.611 · 1 distinct chain · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Perforin-1 | protein | 122 | 0% helix, 54% strand | P10820 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4Y1S · Structural basis for CA2+-mediated interaction of the perforin C2 domain with lipid… · the same entry in another collection · chain A against A, TM-score 1.00
- P10820 · AlphaFold monomer V2.0 prediction for perforin-1 (P10820) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P10820
- Elsewhere: RCSB PDB 4Y1S · PDBe 4Y1S · UniProt P10820
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.