Research workbench
Structure of human liver fbpase complexed with covalent allosteric inhibitor
Analyse Structure of human liver fbpase complexed with covalent allosteric inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LS5
- Type
- protein
- Length
- 1,297 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase 1
- UniProt
- Q2TU34
- Ligands
- AMP, EUF, MG
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Fructose-1,6-bisphosphatase 1 | protein | 327 | 37% helix, 23% strand | Q2TU34 |
| B | Fructose-1,6-bisphosphatase 1 | protein | 323 | 38% helix, 24% strand | Q2TU34 |
| C | Fructose-1,6-bisphosphatase 1 | protein | 320 | 39% helix, 25% strand | Q2TU34 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 4 copies · chains A, B, C, D
- EUF · 2-(ethyldisulfanyl)-1,3-benzothiazole · ligand · chains A, B
- MG · Magnesium ion · metal · 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, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 818 | 0.88 | 0.90 | 83 | empty |
| 2 | 112 | 0.67 | 0.90 | 24 | empty |
| 3 | 59 | 0.56 | 0.89 | 16 | empty |
| 4 | 194 | 0.55 | 0.79 | 29 | AMP |
| 5 | 55 | 0.52 | 0.87 | 22 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2452 Ų buried · 33 hydrogen bonds · protein-protein
- C–D · 2377 Ų buried · 36 hydrogen bonds · protein-protein
- A–C · 1271 Ų buried · 25 hydrogen bonds · protein-protein
- B–D · 1259 Ų buried · 29 hydrogen bonds · protein-protein
- A–D · 558 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6LS5 · Structure of human liver FBPase complexed with covalent 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
- Every structure of UniProt Q2TU34
- Elsewhere: RCSB PDB 6LS5 · PDBe 6LS5 · UniProt Q2TU34
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