Research workbench
Crystal structure of fructose-1,6-bisphosphate aldolase in thermus caldophilus
Analyse Crystal structure of fructose-1,6-bisphosphate aldolase in thermus caldophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FJK
- Type
- protein
- Length
- 1,192 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase
- EC
- 4.1.2.13
- UniProt
- Q703I2
- Ligands
- 13P
- Pockets
- 14 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 305 | 50% helix, 13% strand | Q703I2 |
| B | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 298 | 50% helix, 14% strand | Q703I2 |
| C | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 299 | 49% helix, 14% strand | Q703I2 |
| D | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 290 | 51% helix, 14% strand | Q703I2 |
Ligands and binding sites
- 13P · 1,3-dihydroxyacetonephosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 954 | 0.82 | 0.84 | 81 | empty |
| 2 | 159 | 0.50 | 0.78 | 24 | 13P |
| 3 | 93 | 0.42 | 0.79 | 24 | 13P |
| 4 | 126 | 0.42 | 0.76 | 16 | empty |
| 5 | 79 | 0.42 | 0.79 | 15 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1961 Ų buried · 36 hydrogen bonds · protein-protein
- C–D · 1958 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 641 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 583 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 275 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 modified (engineered).
Compared structures
- 2FJK · Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus · the same entry in another collection · chain D against D, TM-score 1.00
- Q703I2 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase (Q703I2) · a predicted model of the same protein · chain D against A, TM-score 0.99
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 Q703I2
- Elsewhere: RCSB PDB 2FJK · PDBe 2FJK · UniProt Q703I2
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