Research workbench
Cryo-EM structure of the drosophila CTP synthase substrate-bound filament
Analyse Cryo-EM structure of the drosophila CTP synthase substrate-bound filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L6Z
- Type
- protein
- Length
- 4,496 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CTP synthase
- EC
- 6.3.4.2
- UniProt
- Q9VUL1
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 1 distinct chain · 31% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, A, B, C, H, E, F, G | CTP synthase (EC 6.3.4.2) | protein | 562 | 31% helix, 15% strand | Q9VUL1 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 670 | 0.86 | 0.91 | 96 | empty |
| 2 | 352 | 0.84 | 0.93 | 77 | empty |
| 3 | 429 | 0.83 | 0.90 | 66 | empty |
| 4 | 1064 | 0.82 | 0.83 | 93 | empty |
| 5 | 261 | 0.82 | 0.93 | 37 | empty |
Interfaces
16 interfaces between chains.
- A–B · 1375 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 1373 Ų buried · 8 hydrogen bonds · protein-protein
- D–C · 1354 Ų buried · 9 hydrogen bonds · protein-protein
- H–G · 1353 Ų buried · 9 hydrogen bonds · protein-protein
- H–E · 1134 Ų buried · 8 hydrogen bonds · protein-protein
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 Q9VUL1
- Elsewhere: RCSB PDB 6L6Z · PDBe 6L6Z · UniProt Q9VUL1
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