Research workbench
Human muscle fructose-1,6-bisphosphate aldolase
Analyse Human muscle fructose-1,6-bisphosphate aldolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KY6
- Type
- protein
- Length
- 1,318 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
- P04075
- Pockets
- 15 · best druggability 0.88
Structure
x-ray diffraction · 4 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 | 324 | 45% helix, 17% strand | P04075 |
| B | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 335 | 45% helix, 16% strand | P04075 |
| C | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 334 | 45% helix, 16% strand | P04075 |
| D | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 325 | 46% helix, 17% strand | P04075 |
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 | 972 | 0.88 | 0.90 | 117 | empty |
| 2 | 566 | 0.80 | 0.86 | 83 | empty |
| 3 | 598 | 0.80 | 0.86 | 85 | empty |
| 4 | 171 | 0.67 | 0.87 | 46 | empty |
| 5 | 162 | 0.64 | 0.86 | 44 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1657 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1626 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1286 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 1256 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 128 Ų buried · 3 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 5KY6 · PDBe 5KY6 · UniProt P04075
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