Research workbench
Isomerase domain of glucosamine 6-phosphate synthase complexed with 2- amino-2-deoxyglucitol 6-phosphate
Analyse Isomerase domain of glucosamine 6-phosphate synthase complexed with 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MOS
- Type
- protein
- Length
- 367 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucosamine 6-phosphate synthase
- EC
- 2.6.1.16
- UniProt
- P17169
- Ligands
- AGP, NA, SO4
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucosamine 6-phosphate synthase (EC 2.6.1.16) | protein | 367 | 49% helix, 17% strand | P17169 |
Ligands and binding sites
- AGP · 2-deoxy-2-amino glucitol-6-phosphate · ligand · chains A
- NA · Sodium ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.59 | 0.82 | 26 | AGP |
| 2 | 86 | 0.40 | 0.78 | 19 | NA, MES |
Compared structures
- 1MOS · Isomerase domain of glucosamine 6-phosphate synthase complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P17169 · AlphaFold monomer V2.0 prediction for glutamine--fructose-6-phosphate aminotransferase… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P17169
- Elsewhere: RCSB PDB 1MOS · PDBe 1MOS · UniProt P17169
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