Research workbench
Crystal structure of glucosamine 6-phosphate deaminase from pyrococcus furiosus
Analyse Crystal structure of glucosamine 6-phosphate deaminase from pyrococcus furiosus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CB0
- Type
- protein
- Length
- 653 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucosamine-fructose-6-phosphate aminotransferase
- UniProt
- Q8U3U3
- Pockets
- 8 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucosamine-fructose-6-phosphate aminotransferase | protein | 320 | 47% helix, 17% strand | Q8U3U3 |
| B | Glucosamine-fructose-6-phosphate aminotransferase | protein | 333 | 45% helix, 16% strand | Q8U3U3 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 518 | 0.88 | 0.94 | 54 | empty |
| 2 | 140 | 0.76 | 0.94 | 27 | empty |
| 3 | 93 | 0.67 | 0.91 | 22 | empty |
| 4 | 208 | 0.62 | 0.82 | 27 | empty |
| 5 | 84 | 0.61 | 0.89 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2541 Ų buried · 40 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 2CB0 · Crystal structure of glucosamine 6-phosphate deaminase from Pyrococcus furiosus · 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 Q8U3U3
- Elsewhere: RCSB PDB 2CB0 · PDBe 2CB0 · UniProt Q8U3U3
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