MolNFT v1 · #69664 · protein
Crystal structure of fructose-1,6-bisphosphate aldolase from babesia bovis at 2.1A resolution
3KX6 · Fructose-bisphosphate aldolase: “Crystal structure of fructose-1,6-bisphosphate aldolase from babesia bovis at 2.1A resolution”. X-ray diffraction, 15 pockets (best druggability 0.78). MolNFT v1 #69664 on GenesisL1: 3D structure…
- PDB
- 3KX6
- Type
- protein
- Length
- 1,373 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase
- EC
- 4.1.2.13
- UniProt
- A7AV51
- Pockets
- 15 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 344 | 47% helix, 16% strand | A7AV51 |
| B | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 343 | 48% helix, 16% strand | A7AV51 |
| C | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 343 | 47% helix, 16% strand | A7AV51 |
| D | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 343 | 47% helix, 16% strand | A7AV51 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 7 copies · chains A, B, D, C
- CIT · Citric acid · additive · 3 copies · chains A, B, C
- EDO · 1,2-ethanediol · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 355 | 0.78 | 0.88 | 46 | empty |
| 2 | 197 | 0.76 | 0.91 | 39 | PEG |
| 3 | 168 | 0.75 | 0.92 | 34 | PEG |
| 4 | 131 | 0.65 | 0.88 | 41 | empty |
| 5 | 211 | 0.63 | 0.83 | 27 | CIT |
Interfaces
6 interfaces between chains.
- B–C · 1230 Ų buried · 21 hydrogen bonds · protein-protein
- A–D · 1154 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1088 Ų buried · 18 hydrogen bonds · protein-protein
- C–D · 999 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 157 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3KX6 · Crystal structure of fructose-1,6-bisphosphate aldolase from Babesia bovis at 2.1A… · the same entry in another collection · chain A against A, 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 A7AV51
- Elsewhere: RCSB PDB 3KX6 · PDBe 3KX6 · UniProt A7AV51
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