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Ionic interactions with parvalbumins. crystal structure determination of pike 4.10 parvalbumin in four different ionic environments
Analyse Ionic interactions with parvalbumins. crystal structure determination of pike… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PAL
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Parvalbumin
- UniProt
- P02619
- Ligands
- ACE, CA, NH4
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Parvalbumin | protein | 107 | 56% helix, 4% strand | P02619 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- NH4 · Ammonium ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1PAL · Ionic interactions with parvalbumins. crystal structure determination of pike 4.10… · the same entry in another collection · chain A against A, TM-score 1.00
- P02619 · AlphaFold monomer V2.0 prediction for parvalbumin beta (P02619) · 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 P02619
- Elsewhere: RCSB PDB 1PAL · PDBe 1PAL · UniProt P02619
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