Research workbench
Structure of the R75A mutant of rat alpha-Parvalbumin
Analyse Structure of the R75A mutant of rat alpha-Parvalbumin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F45
- Type
- protein
- Length
- 109 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Rattus norvegicus
- Molecule
- Parvalbumin alpha
- UniProt
- P02625
- Ligands
- CA, SO4
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 58% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Parvalbumin alpha | protein | 109 | 58% helix, 2% strand | P02625 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P02625
- Elsewhere: RCSB PDB 3F45 · PDBe 3F45 · UniProt P02625
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.