Research workbench
Crystal structure of human gfat-1 S205D
Analyse Crystal structure of human gfat-1 S205D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NDL
- Type
- protein
- Length
- 1,313 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 2 of glutamine-fructose-6-phosphate aminotransferase [isomerizing] 1
- EC
- 2.6.1.16
- Ligands
- G6Q, GLU
- Pockets
- 16 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 2 of glutamine-fructose-6-phosphate aminotransferase [isomerizing] 1 (EC 2.6.1.16) | protein | 658 | 38% helix, 25% strand | — |
| B | Isoform 2 of glutamine-fructose-6-phosphate aminotransferase [isomerizing] 1 (EC 2.6.1.16) | protein | 655 | 38% helix, 24% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 652 | 0.87 | 0.91 | 64 | empty |
| 2 | 119 | 0.78 | 0.97 | 30 | G6Q |
| 3 | 1120 | 0.76 | 0.78 | 98 | G6Q, GLU |
| 4 | 413 | 0.72 | 0.83 | 45 | empty |
| 5 | 256 | 0.66 | 0.83 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 2775 Ų buried · 52 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 7NDL · Crystal structure of human GFAT-1 S205D · 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
- Elsewhere: RCSB PDB 7NDL · PDBe 7NDL
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