Research workbench
Solution structure of human alpha-parvalbumin refined with a paramagnetism-based strategy
Analyse Solution structure of human alpha-parvalbumin refined with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RJV
- Type
- protein
- Length
- 110 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Parvalbumin alpha
- UniProt
- P20472
- Ligands
- CA
Structure
solution nmr · 1 distinct chain · 52% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Parvalbumin alpha | protein | 110 | 52% helix, 2% strand | P20472 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1RJV · Solution Structure of Human alpha-Parvalbumin refined with a paramagnetism-based strategy · the same entry in another collection · chain A against A, TM-score 1.00
- P20472 · AlphaFold monomer V2.0 prediction for parvalbumin alpha (P20472) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 P20472
- Elsewhere: RCSB PDB 1RJV · PDBe 1RJV · UniProt P20472
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