Research workbench
Crystal structure of CBARA1 in the CA2+ binding form
Analyse Crystal structure of CBARA1 in the CA2+ binding form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NSD
- Type
- protein
- Length
- 573 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium uptake protein 1, mitochondrial
- UniProt
- Q9BPX6
- Ligands
- CA, CL
- Pockets
- 9 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcium uptake protein 1, mitochondrial | protein | 290 | 57% helix, 8% strand | Q9BPX6 |
| B | Calcium uptake protein 1, mitochondrial | protein | 283 | 54% helix, 10% strand | Q9BPX6 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 685 | 0.74 | 0.80 | 59 | empty |
| 2 | 471 | 0.72 | 0.81 | 47 | MPD |
| 3 | 150 | 0.54 | 0.80 | 17 | empty |
| 4 | 102 | 0.48 | 0.80 | 15 | MPD |
| 5 | 142 | 0.42 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 457 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4NSD · Crystal Structure of CBARA1 in the Ca2+ Binding Form · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BPX6 · AlphaFold monomer V2.0 prediction for calcium uptake protein 1, mitochondrial (Q9BPX6) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 Q9BPX6
- Elsewhere: RCSB PDB 4NSD · PDBe 4NSD · UniProt Q9BPX6
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