Research workbench
Membrane protein
Analyse Membrane protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KZO
- Type
- protein
- Length
- 967 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Voltage-dependent T-type calcium channel subunit alpha-1G
- UniProt
- O43497
- Ligands
- 3PE, Y01, NAG, CA
- Pockets
- 19 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Voltage-dependent T-type calcium channel subunit alpha-1G | protein | 967 | 69% helix, 2% strand | O43497 |
Ligands and binding sites
- 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · ligand · 13 copies · chains A
- Y01 · Cholesterol hemisuccinate · ligand · 2 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1191 | 0.83 | 0.84 | 94 | CA, 3PE |
| 2 | 683 | 0.67 | 0.76 | 64 | CA |
| 3 | 51 | 0.66 | 0.95 | 12 | empty |
| 4 | 286 | 0.64 | 0.81 | 34 | empty |
| 5 | 269 | 0.63 | 0.81 | 39 | empty |
Modifications
Observed in the structure: 5 glycan, 4 disulfide (N-glycosylation, disulfide).
Compared structures
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 O43497
- Elsewhere: RCSB PDB 6KZO · PDBe 6KZO · UniProt O43497
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