Research workbench
Human aldolase a wild type
Analyse Human aldolase a wild type in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XMH
- Type
- protein
- Length
- 707 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase a
- EC
- 4.1.2.13
- UniProt
- P04075
- Ligands
- PO4
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 356 | 46% helix, 15% strand | P04075 |
| B | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 351 | 45% helix, 16% strand | P04075 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
- GOL · Glycerol · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 617 | 0.76 | 0.82 | 68 | GOL |
| 2 | 412 | 0.70 | 0.82 | 55 | PO4 |
| 3 | 170 | 0.62 | 0.84 | 35 | PO4 |
| 4 | 162 | 0.59 | 0.83 | 26 | empty |
| 5 | 150 | 0.54 | 0.81 | 29 | GOL |
Interfaces
1 interface between chains.
- A–B · 837 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
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 P04075
- Elsewhere: RCSB PDB 6XMH · PDBe 6XMH · UniProt P04075
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.