Research workbench
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from escherichia COLI at 2.1 ångströms resolution
Analyse Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DEA
- 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
- P0A759
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.68
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 | P0A759 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 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 | 192 | 0.68 | 0.87 | 28 | PO4 |
| 2 | 204 | 0.67 | 0.85 | 35 | PO4 |
| 3 | 108 | 0.36 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 523 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1DEA · Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from escherichia… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A759 · AlphaFold monomer V2.0 prediction for glucosamine-6-phosphate deaminase (P0A759) · 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 P0A759
- Elsewhere: RCSB PDB 1DEA · PDBe 1DEA · UniProt P0A759
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