MolNFT v1 · #135007 · protein
Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor naphthalene 2,6-bisphosphate
5TLZ · Fructose-bisphosphate aldolase a: “Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor naphthalene…”. X-ray diffraction, 1 ligand (N26), 17 pockets (best druggability 0.85). MolNFT v1 #135007 on…
- PDB
- 5TLZ
- Type
- protein
- Length
- 1,385 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
- P00883
- Ligands
- N26
- Pockets
- 17 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 346 | 47% helix, 16% strand | P00883 |
| C | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 348 | 47% helix, 16% strand | P00883 |
| D | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 345 | 47% helix, 16% strand | P00883 |
Ligands and binding sites
- N26 · naphthalene-2,6-diyl bis[dihydrogen (phosphate)] · ligand · 4 copies · chains A, B, C, D
- GOL · Glycerol · additive · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 689 | 0.85 | 0.89 | 91 | empty |
| 2 | 411 | 0.83 | 0.91 | 57 | empty |
| 3 | 396 | 0.83 | 0.91 | 56 | empty |
| 4 | 156 | 0.67 | 0.88 | 47 | GOL |
| 5 | 305 | 0.64 | 0.81 | 39 | N26 |
Interfaces
6 interfaces between chains.
- A–D · 1223 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1205 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1123 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1118 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 130 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5TLZ · Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor… · the same entry in another collection · chain D against D, TM-score 1.00
- P00883 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase a (P00883) · a predicted model of the same protein · chain D against A, TM-score 0.99
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 P00883
- Elsewhere: RCSB PDB 5TLZ · PDBe 5TLZ · UniProt P00883
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.