Research workbench
Human aldolase a I98F
Analyse Human aldolase a I98F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XMO
- Type
- protein
- Length
- 706 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
- 12 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 353 | 44% helix, 16% strand | P04075 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
- GOL · Glycerol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.63 | 0.89 | 28 | PO4 |
| 2 | 143 | 0.63 | 0.85 | 31 | GOL |
| 3 | 250 | 0.58 | 0.79 | 37 | PO4, GOL |
| 4 | 153 | 0.57 | 0.82 | 28 | empty |
| 5 | 98 | 0.53 | 0.84 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 908 Ų buried · 12 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 6XMO · PDBe 6XMO · UniProt P04075
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