Research workbench
Structural and functional relationships between the lectin and arm domains of calreticulin
Analyse Structural and functional relationships between the lectin and arm domains of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RG0
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calreticulin
- UniProt
- P14211
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calreticulin | protein | 292 | 14% helix, 39% strand | P14211 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3RG0 · Structural and functional relationships between the lectin and arm domains of calreticulin · the same entry in another collection · chain A against A, TM-score 1.00
- P14211 · AlphaFold monomer V2.0 prediction for calreticulin (P14211) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P14211
- Elsewhere: RCSB PDB 3RG0 · PDBe 3RG0 · UniProt P14211
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