Research workbench
C153S mutant of pea fructose-1,6-bisphosphatase
Analyse C153S mutant of pea fructose-1,6-bisphosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DBZ
- Type
- protein
- Length
- 1,286 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase
- EC
- 3.1.3.11
- UniProt
- P46275
- Pockets
- 17 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 317 | 38% helix, 25% strand | P46275 |
| B | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 326 | 38% helix, 23% strand | P46275 |
| C | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 323 | 37% helix, 24% strand | P46275 |
| D | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 320 | 39% helix, 23% strand | P46275 |
Pockets
17 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 584 | 0.85 | 0.90 | 59 | empty |
| 2 | 222 | 0.67 | 0.85 | 27 | empty |
| 3 | 245 | 0.66 | 0.83 | 30 | empty |
| 4 | 409 | 0.66 | 0.79 | 56 | empty |
| 5 | 233 | 0.66 | 0.84 | 26 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2283 Ų buried · 30 hydrogen bonds · protein-protein
- A–B · 2271 Ų buried · 29 hydrogen bonds · protein-protein
- B–C · 1007 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 883 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 74 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1DBZ · C153S mutant of pea fructose-1,6-bisphosphatase · the same entry in another collection · chain D against D, TM-score 1.00
- P46275 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase, chloroplastic (P46275) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P46275
- Elsewhere: RCSB PDB 1DBZ · PDBe 1DBZ · UniProt P46275
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