Research workbench
Dipeptide gly-pro binds to a glycolytic enzyme fructose bisphosphate aldolase
Analyse Dipeptide gly-pro binds to a glycolytic enzyme fructose bisphosphate aldolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RS1
- Type
- protein
- Length
- 1,348 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase 6, cytosolic
- EC
- 4.1.2.13
- UniProt
- Q9SJQ9
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Fructose-bisphosphate aldolase 6, cytosolic (EC 4.1.2.13) | protein | 337 | 47% helix, 16% strand | Q9SJQ9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 9 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 787 | 0.79 | 0.83 | 87 | empty |
| 2 | 355 | 0.71 | 0.84 | 45 | empty |
| 3 | 479 | 0.70 | 0.80 | 60 | SO4 |
| 4 | 545 | 0.70 | 0.79 | 75 | SO4 |
| 5 | 194 | 0.63 | 0.83 | 24 | empty |
Interfaces
6 interfaces between chains.
- B–C · 687 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 680 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 325 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 303 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 158 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6RS1 · Dipeptide Gly-Pro binds to a glycolytic enzyme fructose bisphosphate aldolase · the same entry in another collection · chain D against D, TM-score 1.00
- Q9SJQ9 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase 6, cytosolic (Q9SJQ9) · a predicted model of the same protein · 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 Q9SJQ9
- Elsewhere: RCSB PDB 6RS1 · PDBe 6RS1 · UniProt Q9SJQ9
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