Research workbench
Structural basis for CA2+ selectivity of a voltage-gated calcium channel
Analyse Structural basis for CA2+ selectivity of a voltage-gated calcium channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MTG
- Type
- protein
- Length
- 876 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ion transport protein
- UniProt
- A8EVM5
- Ligands
- PX4, CA
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Ion transport protein | protein | 219 | 79% helix, 0% strand | A8EVM5 |
Ligands and binding sites
- PX4 · 1,2-dimyristoyl-sn-glycero-3-phosphocholine · ligand · 16 copies · chains A, B, C, D
- CA · Calcium ion · metal · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 747 | 0.83 | 0.86 | 75 | CA, PX4 |
| 2 | 199 | 0.56 | 0.78 | 22 | empty |
| 3 | 120 | 0.55 | 0.82 | 17 | empty |
| 4 | 194 | 0.53 | 0.78 | 30 | empty |
| 5 | 85 | 0.52 | 0.83 | 15 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1547 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 1542 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1541 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 1511 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 4MTG · Structural Basis for Ca2+ Selectivity of a Voltage-gated Calcium Channel · 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 A8EVM5
- Elsewhere: RCSB PDB 4MTG · PDBe 4MTG · UniProt A8EVM5
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