Research workbench
Structure of human liver fpbase complexed with a novel benzoxazole as allosteric inhibitor
Analyse Structure of human liver fpbase complexed with a novel benzoxazole as… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FHY
- Type
- protein
- Length
- 1,268 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
- Ligands
- A37, MG
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, H, L | Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) | protein | 317 | 38% helix, 27% strand | — |
Ligands and binding sites
- A37 · 2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide · ligand · 4 copies · chains A, L, D, H
- MG · Magnesium ion · metal · 4 copies · chains A, D, H, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1003 | 0.84 | 0.85 | 88 | empty |
| 2 | 217 | 0.62 | 0.82 | 33 | A37 |
| 3 | 110 | 0.58 | 0.86 | 19 | A37 |
| 4 | 174 | 0.51 | 0.78 | 27 | MG |
| 5 | 204 | 0.50 | 0.77 | 37 | MG |
Interfaces
6 interfaces between chains.
- A–D · 2410 Ų buried · 38 hydrogen bonds · protein-protein
- H–L · 2402 Ų buried · 34 hydrogen bonds · protein-protein
- A–L · 1260 Ų buried · 25 hydrogen bonds · protein-protein
- D–H · 1260 Ų buried · 27 hydrogen bonds · protein-protein
- D–L · 428 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2FHY · Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor · 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
- Elsewhere: RCSB PDB 2FHY · PDBe 2FHY
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