Research workbench
2.0 a crystal structure of the CAV1.2 iq domain-CA/CAM complex
Analyse 2.0 a crystal structure of the CAV1.2 iq domain-CA/CAM complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BE6
- Type
- protein
- Length
- 482 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin 2; Voltage-dependent L-type calcium channel alpha-1C subunit
- UniProt
- Q53S29, Q13933
- Ligands
- CA, NI
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 6 distinct chains · 63% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin 2 | protein | 141 | 62% helix, 6% strand | Q53S29 |
| D | Voltage-dependent L-type calcium channel alpha-1C subunit | protein | 29 | 76% helix, 0% strand | Q13933 |
| B | Calmodulin 2 | protein | 140 | 62% helix, 6% strand | Q53S29 |
| E | Voltage-dependent L-type calcium channel alpha-1C subunit | protein | 14 | 86% helix, 0% strand | Q13933 |
| C | Calmodulin 2 | protein | 136 | 57% helix, 6% strand | Q53S29 |
| F | Voltage-dependent L-type calcium channel alpha-1C subunit | protein | 22 | 82% helix, 0% strand | Q13933 |
Ligands and binding sites
- CA · Calcium ion · metal · 12 copies · chains A, B, C
- NI · Nickel (II) ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 467 | 0.64 | 0.77 | 41 | empty |
| 2 | 258 | 0.51 | 0.74 | 28 | empty |
| 3 | 114 | 0.45 | 0.77 | 17 | empty |
| 4 | 80 | 0.41 | 0.79 | 17 | empty |
| 5 | 85 | 0.34 | 0.75 | 20 | empty |
Interfaces
5 interfaces between chains.
- A–D · 1617 Ų buried · 10 hydrogen bonds · protein-protein
- C–F · 1572 Ų buried · 12 hydrogen bonds · protein-protein
- B–E · 887 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 388 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 277 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2BE6 · 2.0 A crystal structure of the CaV1.2 IQ domain-Ca/CaM complex · the same entry in another collection · chain A against A, TM-score 1.00
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 Q53S29
- Every structure of UniProt Q13933
- Elsewhere: RCSB PDB 2BE6 · PDBe 2BE6 · UniProt Q53S29 · UniProt Q13933
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