Research workbench
Fructose-1,6-bisphosphate aldolase from leishmania mexicana
Analyse Fructose-1,6-bisphosphate aldolase from leishmania mexicana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QAP
- Type
- protein
- Length
- 1,432 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphate aldolase
- EC
- 4.1.2.13
- UniProt
- Q9U5N6
- Ligands
- PO4
- Pockets
- 15 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) | protein | 358 | 47% helix, 17% strand | Q9U5N6 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 11 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1094 | 0.88 | 0.90 | 139 | empty |
| 2 | 181 | 0.78 | 0.93 | 32 | empty |
| 3 | 354 | 0.60 | 0.77 | 33 | PO4 |
| 4 | 252 | 0.59 | 0.79 | 27 | PO4 |
| 5 | 253 | 0.58 | 0.79 | 28 | PO4 |
Interfaces
6 interfaces between chains.
- B–C · 1594 Ų buried · 22 hydrogen bonds · protein-protein
- A–D · 1560 Ų buried · 24 hydrogen bonds · protein-protein
- B–D · 1521 Ų buried · 28 hydrogen bonds · protein-protein
- A–C · 1498 Ų buried · 30 hydrogen bonds · protein-protein
- A–B · 627 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2QAP · Fructose-1,6-bisphosphate aldolase from Leishmania mexicana · the same entry in another collection · 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 Q9U5N6
- Elsewhere: RCSB PDB 2QAP · PDBe 2QAP · UniProt Q9U5N6
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