Research workbench
Sucrose-phosphate synthase (TLL1590)_27_220_406_426_FROM thermosynechococcus elongatus (twinned)
Analyse Sucrose-phosphate synthase (TLL1590)_27_220_406_426_FROM thermosynechococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LDQ
- Type
- protein
- Length
- 739 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TLL1590 protein
- UniProt
- Q8DIJ5
- Ligands
- SCN
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, A | TLL1590 protein | protein | 187 | 47% helix, 20% strand | Q8DIJ5 |
| B | TLL1590 protein | protein | 184 | 47% helix, 21% strand | Q8DIJ5 |
| C | TLL1590 protein | protein | 181 | 46% helix, 21% strand | Q8DIJ5 |
Ligands and binding sites
- SCN · Thiocyanate ion · ion · 4 copies · chains D, A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1039 | 0.75 | 0.78 | 72 | empty |
| 2 | 302 | 0.61 | 0.79 | 35 | empty |
| 3 | 161 | 0.48 | 0.77 | 27 | empty |
| 4 | 162 | 0.46 | 0.76 | 25 | empty |
| 5 | 138 | 0.44 | 0.76 | 24 | empty |
Interfaces
4 interfaces between chains.
- D–A · 744 Ų buried · 8 hydrogen bonds · protein-protein
- D–C · 404 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 345 Ų buried · 9 hydrogen bonds · protein-protein
- D–B · 206 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6LDQ · Sucrose-phosphate synthase (tll1590)_27_220_406_426_from Thermosynechococcus elongatus… · the same entry in another collection · chain B against B, 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 Q8DIJ5
- Elsewhere: RCSB PDB 6LDQ · PDBe 6LDQ · UniProt Q8DIJ5
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