MolNFT v1 · #71729 · protein
Crystal structure of fructose bisphosphate aldolase from bartonella henselae, bound to fructose bisphosphate
3MMT · Fructose-bisphosphate aldolase: “Crystal structure of fructose bisphosphate aldolase from bartonella henselae, bound to fructose bisphosphate”. X-ray diffraction, 1 ligand (2FP), 14 pockets (best druggability 0.81). MolNFT v1 #71729…
- PDB
- 3MMT
- Type
- protein
- Length
- 1,363 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
- Q8L207
- Ligands
- 2FP
- Pockets
- 14 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 50% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 341 | 50% helix, 15% strand | Q8L207 |
| B | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 340 | 50% helix, 16% strand | Q8L207 |
| C, D | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 341 | 50% helix, 16% strand | Q8L207 |
Ligands and binding sites
- 2FP · 1,6-fructose diphosphate (linear form) · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1141 | 0.81 | 0.82 | 105 | empty |
| 2 | 111 | 0.78 | 0.97 | 26 | empty |
| 3 | 106 | 0.77 | 0.97 | 21 | empty |
| 4 | 79 | 0.74 | 0.97 | 24 | empty |
| 5 | 75 | 0.73 | 0.97 | 28 | empty |
Interfaces
4 interfaces between chains.
- A–D · 1115 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1113 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 746 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 731 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (covalent ligand).
Compared structures
- 3MMT · Crystal structure of fructose bisphosphate aldolase from Bartonella henselae, bound to… · 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 Q8L207
- Elsewhere: RCSB PDB 3MMT · PDBe 3MMT · UniProt Q8L207
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