MolNFT v1 · #93819 · protein
Crystal structure of human muscle fructose-1,6-bisphosphatase Q32R mutant complex with AMP
4HE2 · Fructose-1,6-bisphosphatase isozyme 2: “Crystal structure of human muscle fructose-1,6-bisphosphatase Q32R mutant complex with AMP”. X-ray diffraction, 5 ligands (AMP, MG, ZN), 2 pockets (best druggability 0.50). MolNFT v1 #93819 on…
- PDB
- 4HE2
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase isozyme 2
- EC
- 3.1.3.11
- UniProt
- O00757
- Ligands
- AMP, MG, ZN, PO3, CL
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase isozyme 2 (EC 3.1.3.11) | protein | 308 | 38% helix, 26% strand | O00757 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- MG · Magnesium ion · metal · 3 copies · chains A
- ZN · Zinc ion · metal · chains A
- PO3 · Phosphite ion · ion · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.50 | 0.81 | 24 | AMP |
| 2 | 95 | 0.42 | 0.78 | 21 | PO3, ZN |
Compared structures
- 4HE2 · Crystal structure of human muscle fructose-1,6-bisphosphatase Q32R mutant complex with AMP · the same entry in another collection · chain A against A, TM-score 1.00
- O00757 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase isozyme 2 (O00757) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O00757
- Elsewhere: RCSB PDB 4HE2 · PDBe 4HE2 · UniProt O00757
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