Research workbench
Crystal structure of the alpha parvalbumin from thornback ray
Analyse Crystal structure of the alpha parvalbumin from thornback ray in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 9BAR
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.75
- Source
- Raja clavata
- Molecule
- Parvalbumin alpha
- UniProt
- P02630
- Ligands
- CA, SO4
Structure
x-ray diffraction · resolution 1.75 · 1 distinct chain · 60% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Parvalbumin alpha | protein | 108 | 60% helix, 2% strand | P02630 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P02630 · AlphaFold monomer V2.0 prediction for parvalbumin alpha (P02630) · 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 P02630
- Elsewhere: RCSB PDB 9BAR · PDBe 9BAR · UniProt P02630
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