Research workbench
The crystal structure of calcineurin B homologous proein 1 (CHP1)
Analyse The crystal structure of calcineurin B homologous proein 1 (CHP1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CT9
- Type
- protein
- Length
- 383 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-binding protein P22
- UniProt
- P61023
- Ligands
- CA
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcium-binding protein P22 | protein | 185 | 59% helix, 4% strand | P61023 |
| B | Calcium-binding protein P22 | protein | 198 | 62% helix, 4% strand | P61023 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B
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 | 206 | 0.84 | 0.97 | 45 | empty |
| 2 | 141 | 0.43 | 0.76 | 24 | empty |
| 3 | 56 | 0.33 | 0.77 | 15 | empty |
| 4 | 69 | 0.29 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1621 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2CT9 · The crystal structure of calcineurin B homologous proein 1 (CHP1) · the same entry in another collection · chain A against A, TM-score 1.00
- P61023 · AlphaFold monomer V2.0 prediction for calcineurin B homologous protein 1 (P61023) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P61023
- Elsewhere: RCSB PDB 2CT9 · PDBe 2CT9 · UniProt P61023
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