Research workbench
Glucosamine 6-phosphate deaminase complexed with the allosteric activator N-acetyl-glucosamine-6-phosphate
Analyse Glucosamine 6-phosphate deaminase complexed with the allosteric activator… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HOT
- Type
- protein
- Length
- 532 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucosamine 6-phosphate deaminase
- EC
- 5.3.1.10
- UniProt
- P09375
- Ligands
- 16G, PO4
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glucosamine 6-phosphate deaminase (EC 5.3.1.10) | protein | 266 | 43% helix, 17% strand | P09375 |
Ligands and binding sites
- 16G · 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 236 | 0.70 | 0.86 | 38 | PO4 |
| 2 | 226 | 0.67 | 0.84 | 39 | PO4 |
| 3 | 118 | 0.37 | 0.74 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 514 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1HOT · Glucosamine 6-phosphate deaminase complexed with the allosteric activator… · 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 P09375
- Elsewhere: RCSB PDB 1HOT · PDBe 1HOT · UniProt P09375
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