MolNFT v1 · #4461 · protein
Structure of fructose-bisphosphate aldolase
1DOS · Aldolase class II: “Structure of fructose-bisphosphate aldolase”. X-ray diffraction, 2 ligands (ZN, NH4), 6 pockets (best druggability 0.72). MolNFT v1 #4461 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DOS
- Type
- protein
- Length
- 716 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldolase class II
- EC
- 4.1.2.13
- UniProt
- P0AB71
- Ligands
- ZN, NH4
- Pockets
- 6 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aldolase class II (EC 4.1.2.13) | protein | 358 | 50% helix, 13% strand | P0AB71 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 488 | 0.72 | 0.82 | 78 | empty |
| 2 | 316 | 0.67 | 0.82 | 65 | empty |
| 3 | 288 | 0.59 | 0.79 | 40 | empty |
| 4 | 77 | 0.37 | 0.77 | 16 | empty |
| 5 | 56 | 0.36 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2428 Ų buried · 20 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 P0AB71
- Elsewhere: RCSB PDB 1DOS · PDBe 1DOS · UniProt P0AB71
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