Research workbench
Crystal structure of human gfat-1 G461E after udp-glcnac soaking
Analyse Crystal structure of human gfat-1 G461E after udp-glcnac soaking in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SVQ
- Type
- protein
- Length
- 1,292 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q06210
- Ligands
- G6Q
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 652 | — | Q06210 |
| B | — | protein | 640 | — | Q06210 |
Ligands and binding sites
- G6Q · Glucose-6-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6SVQ · Crystal structure of human GFAT-1 G461E after UDP-GlcNAc soaking · the same entry in another collection · chain B against B, TM-score 1.00
- Q06210 · AlphaFold monomer V2.0 prediction for glutamine--fructose-6-phosphate aminotransferase… · a predicted model of the same protein · chain B 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 Q06210
- Elsewhere: RCSB PDB 6SVQ · PDBe 6SVQ · UniProt Q06210
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