Research workbench
The crystal structure of arabidopsis thaliana CAR4 in complex with two calcium ions
Analyse The crystal structure of arabidopsis thaliana CAR4 in complex with two calcium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4V29
- Type
- protein
- Length
- 330 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AT3G17980
- UniProt
- Q9LVH4
- Ligands
- CA
- Pockets
- 6 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | AT3G17980 | protein | 165 | 4% helix, 47% strand | Q9LVH4 |
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
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.52 | 0.78 | 24 | empty |
| 2 | 220 | 0.52 | 0.76 | 29 | empty |
| 3 | 124 | 0.40 | 0.75 | 15 | empty |
| 4 | 55 | 0.38 | 0.80 | 15 | empty |
| 5 | 81 | 0.37 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 632 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4V29 · The crystal structure of Arabidopsis thaliana CAR4 in complex with two calcium ions · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LVH4 · AlphaFold monomer V2.0 prediction for protein C2-domain aba-related 4 (Q9LVH4) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9LVH4
- Elsewhere: RCSB PDB 4V29 · PDBe 4V29 · UniProt Q9LVH4
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