Research workbench
Indole-2-carboxylic acid derivatives as allosteric inhibitors of fructose-1,6-bisphosphatase
Analyse Indole-2-carboxylic acid derivatives as allosteric inhibitors of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EZF
- Type
- protein
- Length
- 1,285 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase 1
- EC
- 3.1.3.11
- UniProt
- P09467
- Ligands
- 0KI, FBP
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 318 | 39% helix, 25% strand | P09467 |
| B | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 318 | 36% helix, 26% strand | P09467 |
| C | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 320 | 37% helix, 25% strand | P09467 |
| D | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 329 | 37% helix, 24% strand | P09467 |
Ligands and binding sites
- 0KI · 7-chloranyl-5-ethyl-3-(3-hydroxy-3-oxopropyl)-1H-indole-2-carboxylic acid · ligand · 4 copies · chains A, B, C, D
- FBP · 1,6-di-O-phosphono-beta-D-fructofuranose · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1029 | 0.86 | 0.87 | 98 | empty |
| 2 | 60 | 0.73 | 0.99 | 23 | empty |
| 3 | 312 | 0.62 | 0.79 | 44 | 0KI |
| 4 | 237 | 0.61 | 0.81 | 44 | FBP |
| 5 | 354 | 0.60 | 0.77 | 45 | 0KI |
Interfaces
6 interfaces between chains.
- A–B · 2542 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 2537 Ų buried · 37 hydrogen bonds · protein-protein
- A–C · 1253 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 1051 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 461 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7EZF · Indole-2-carboxylic acid derivatives as allosteric inhibitors of… · the same entry in another collection · chain D against D, TM-score 1.00
- P09467 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P09467) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P09467
- Elsewhere: RCSB PDB 7EZF · PDBe 7EZF · UniProt P09467
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