Research workbench
Pike parvalbumin (pi 4.10) at low temperature (100K) and atomic resolution (0.91 a).
Analyse Pike parvalbumin (pi 4.10) at low temperature (100K) and atomic resolution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PVB
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (parvalbumin)
- UniProt
- P02619
- Ligands
- ACE, CA, NH4
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (parvalbumin) | protein | 107 | 57% helix, 2% 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
- FMT · Formic acid · additive · 2 copies · 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
- 2PVB · Pike parvalbumin (pi 4.10) at low temperature (100K) and atomic resolution (0.91 a). · 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 0.97
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 2PVB · PDBe 2PVB · UniProt P02619
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