Research workbench
Phosphate ions in fructose-1,6-bisphosphate aldolase from rabbit muscle
Analyse Phosphate ions in fructose-1,6-bisphosphate aldolase from rabbit muscle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QUV
- Type
- protein
- Length
- 1,431 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase a
- EC
- 4.1.2.13
- UniProt
- P00883
- Ligands
- PO4
- Pockets
- 18 · best druggability 0.89
Structure
x-ray diffraction · 3 distinct chains · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 351 | 46% helix, 15% strand | P00883 |
| B, D | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 363 | 44% helix, 14% strand | P00883 |
| C | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 354 | 45% helix, 15% strand | P00883 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 7 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1052 | 0.89 | 0.90 | 115 | empty |
| 2 | 714 | 0.81 | 0.85 | 94 | PO4 |
| 3 | 632 | 0.81 | 0.85 | 85 | PO4 |
| 4 | 110 | 0.66 | 0.90 | 36 | empty |
| 5 | 159 | 0.64 | 0.86 | 53 | empty |
Interfaces
6 interfaces between chains.
- A–D · 1534 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 1528 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1239 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1211 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 100 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2QUV · Phosphate ions in fructose-1,6-bisphosphate aldolase from rabbit muscle · the same entry in another collection · chain D against D, TM-score 1.00
- P00883 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase a (P00883) · a predicted model of the same protein · chain D 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 P00883
- Elsewhere: RCSB PDB 2QUV · PDBe 2QUV · UniProt P00883
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