Research workbench
Crystal structure of fructose-1,6-bisphosphatase, type I, from stenotrophomonas maltophilia K279A
Analyse Crystal structure of fructose-1,6-bisphosphatase, type I, from stenotrophomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7K74
- Type
- protein
- Length
- 1,294 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase class 1
- EC
- 3.1.3.11
- UniProt
- B2FU10
- Ligands
- PO4
- Pockets
- 12 · best druggability 0.89
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Fructose-1,6-bisphosphatase class 1 (EC 3.1.3.11) | protein | 324 | 40% helix, 23% strand | B2FU10 |
| C | Fructose-1,6-bisphosphatase class 1 (EC 3.1.3.11) | protein | 322 | 40% helix, 23% strand | B2FU10 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1146 | 0.89 | 0.90 | 103 | empty |
| 2 | 207 | 0.55 | 0.79 | 37 | PO4 |
| 3 | 185 | 0.53 | 0.78 | 27 | PO4 |
| 4 | 199 | 0.52 | 0.78 | 32 | PO4 |
| 5 | 184 | 0.49 | 0.77 | 29 | PO4 |
Interfaces
4 interfaces between chains.
- C–D · 2095 Ų buried · 39 hydrogen bonds · protein-protein
- A–B · 2084 Ų buried · 40 hydrogen bonds · protein-protein
- A–C · 842 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 805 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7K74 · Crystal Structure of Fructose-1,6-bisphosphatase, type I, from Stenotrophomonas… · the same entry in another collection · chain D against D, TM-score 1.00
- B2FU10 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase class 1 (B2FU10) · 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 B2FU10
- Elsewhere: RCSB PDB 7K74 · PDBe 7K74 · UniProt B2FU10
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.