MolNFT v1 · #31152 · protein
Human muscle aldolase
2ALD · Fructose-bisphosphate aldolase: “Human muscle aldolase”. X-ray diffraction, 2 pockets (best druggability 0.74). MolNFT v1 #31152 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2ALD
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase
- EC
- 4.1.2.13
- UniProt
- P04075
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 363 | 45% helix, 14% strand | P04075 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 488 | 0.74 | 0.83 | 48 | empty |
| 2 | 177 | 0.58 | 0.82 | 30 | empty |
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 2ALD · PDBe 2ALD · UniProt P04075
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