MolNFT v1 · #171962 · protein
Crystal structure of human gfat-1 R203H
6ZMJ · Glutamine--fructose-6-phosphate aminotransferase…: “Crystal structure of human gfat-1 R203H”. X-ray diffraction, 2 ligands (G6Q, GLU), 13 pockets (best druggability 0.87). MolNFT v1 #171962 on GenesisL1: 3D structure, binding sites…
- PDB
- 6ZMJ
- Type
- protein
- Length
- 1,298 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1
- EC
- 2.6.1.16
- UniProt
- Q06210
- Ligands
- G6Q, GLU
- Pockets
- 13 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (EC 2.6.1.16) | protein | 649 | 39% helix, 25% strand | Q06210 |
| B | Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (EC 2.6.1.16) | protein | 649 | 39% helix, 23% strand | Q06210 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 643 | 0.87 | 0.91 | 61 | empty |
| 2 | 862 | 0.79 | 0.82 | 92 | empty |
| 3 | 116 | 0.78 | 0.97 | 28 | G6Q |
| 4 | 1158 | 0.76 | 0.79 | 109 | G6Q, GLU |
| 5 | 121 | 0.50 | 0.80 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 2641 Ų buried · 50 hydrogen bonds · protein-protein
Compared structures
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 Q06210
- Elsewhere: RCSB PDB 6ZMJ · PDBe 6ZMJ · UniProt Q06210
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