MolNFT v1 · #19569 · protein
Fructose 1,6-bisphosphate aldolase from human liver tissue
1QO5 · Fructose-bisphosphate aldolase B: “Fructose 1,6-bisphosphate aldolase from human liver tissue”. X-ray diffraction, 1 ligand (SO4), 20 pockets (best druggability 0.89). MolNFT v1 #19569 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1QO5
- Type
- protein
- Length
- 6,311 residues
- Chains
- 18
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase B
- EC
- 4.1.2.13
- UniProt
- P05062
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 9 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, M, P | Fructose-bisphosphate aldolase B (EC 4.1.2.13) | protein | 360 | 46% helix, 16% strand | P05062 |
| B | Fructose-bisphosphate aldolase B (EC 4.1.2.13) | protein | 348 | 46% helix, 16% strand | P05062 |
| C | Fructose-bisphosphate aldolase B (EC 4.1.2.13) | protein | 345 | 48% helix, 16% strand | P05062 |
| D, J | Fructose-bisphosphate aldolase B (EC 4.1.2.13) | protein | 356 | 47% helix, 15% strand | P05062 |
| E | Fructose-bisphosphate aldolase B (EC 4.1.2.13) | protein | 354 | 46% helix, 15% strand | P05062 |
| F | Fructose-bisphosphate aldolase B (EC 4.1.2.13) | protein | 353 | 46% helix, 16% strand | P05062 |
| G, I, L, N, O, Q, R | Fructose-bisphosphate aldolase B (EC 4.1.2.13) | protein | 344 | 48% helix, 16% strand | P05062 |
| H | Fructose-bisphosphate aldolase B (EC 4.1.2.13) | protein | 357 | 47% helix, 15% strand | P05062 |
| K | Fructose-bisphosphate aldolase B (EC 4.1.2.13) | protein | 354 | 47% helix, 16% strand | P05062 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 15 copies · chains A, D, E, G, F, J, K, M, P, N, O, R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1146 | 0.89 | 0.90 | 154 | empty |
| 2 | 833 | 0.88 | 0.91 | 121 | empty |
| 3 | 518 | 0.84 | 0.91 | 89 | empty |
| 4 | 456 | 0.83 | 0.90 | 69 | empty |
| 5 | 266 | 0.82 | 0.94 | 56 | empty |
Interfaces
29 interfaces between chains.
- Q–R · 1418 Ų buried · 28 hydrogen bonds · protein-protein
- G–H · 1416 Ų buried · 29 hydrogen bonds · protein-protein
- C–D · 1400 Ų buried · 24 hydrogen bonds · protein-protein
- I–J · 1395 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 1379 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 1QO5 · Fructose 1,6-bisphosphate Aldolase from Human Liver Tissue · the same entry in another collection · chain D against D, TM-score 1.00
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 P05062
- Elsewhere: RCSB PDB 1QO5 · PDBe 1QO5 · UniProt P05062
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