Research workbench
MUNC13-1 C1-C2B-mun-C2C lateral conformation on lipid bilayer surface
Analyse MUNC13-1 C1-C2B-mun-C2C lateral conformation on lipid bilayer surface in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7T7V
- Type
- protein
- Length
- 1,132 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein unc-13 homolog a
- UniProt
- Q4KUS2
- Pockets
- 11 · best druggability 0.61
Structure
electron microscopy · 1 distinct chain · 54% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein unc-13 homolog a | protein | 1132 | 54% helix, 14% strand | Q4KUS2 |
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.61 | 0.78 | 45 | empty |
| 2 | 132 | 0.60 | 0.85 | 34 | empty |
| 3 | 149 | 0.53 | 0.80 | 20 | empty |
| 4 | 163 | 0.50 | 0.78 | 24 | empty |
| 5 | 70 | 0.49 | 0.84 | 21 | empty |
Compared structures
- 7T7V · Munc13-1 C1-C2B-MUN-C2C Lateral conformation on lipid bilayer surface · the same entry in another collection · chain A against A, TM-score 1.00
- Q4KUS2 · AlphaFold monomer V2.0 prediction for protein unc-13 homolog a (Q4KUS2) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 Q4KUS2
- Elsewhere: RCSB PDB 7T7V · PDBe 7T7V · UniProt Q4KUS2
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