Research workbench
Crystal structure of the globular domain of human calreticulin
Analyse Crystal structure of the globular domain of human calreticulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3POS
- Type
- protein
- Length
- 753 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calreticulin
- UniProt
- P27797
- Ligands
- CA
- Pockets
- 4 · best druggability 0.50
Structure
x-ray diffraction · 3 distinct chains · 15% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calreticulin | protein | 249 | 16% helix, 43% strand | P27797 |
| B | Calreticulin | protein | 253 | 15% helix, 42% strand | P27797 |
| C | Calreticulin | protein | 251 | 15% helix, 41% strand | P27797 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.50 | 0.78 | 19 | empty |
| 2 | 203 | 0.48 | 0.75 | 31 | empty |
| 3 | 90 | 0.37 | 0.76 | 20 | empty |
| 4 | 60 | 0.31 | 0.76 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 397 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 382 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 21 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 P27797
- Elsewhere: RCSB PDB 3POS · PDBe 3POS · UniProt P27797
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