6R4H
Crystal structure of human GFAT-1 G451E
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004360 | molecular_function | glutamine-fructose-6-phosphate transaminase (isomerizing) activity |
| A | 0097367 | molecular_function | carbohydrate derivative binding |
| A | 1901135 | biological_process | carbohydrate derivative metabolic process |
| A | 1901137 | biological_process | carbohydrate derivative biosynthetic process |
| B | 0004360 | molecular_function | glutamine-fructose-6-phosphate transaminase (isomerizing) activity |
| B | 0097367 | molecular_function | carbohydrate derivative binding |
| B | 1901135 | biological_process | carbohydrate derivative metabolic process |
| B | 1901137 | biological_process | carbohydrate derivative biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue G6Q A 701 |
| Chain | Residue |
| A | CYS374 |
| A | LYS558 |
| A | GLU561 |
| A | HOH818 |
| A | HOH834 |
| A | HOH874 |
| B | HIS577 |
| A | GLY375 |
| A | THR376 |
| A | SER377 |
| A | SER421 |
| A | GLN422 |
| A | SER423 |
| A | THR426 |
| A | SER474 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue GLU A 702 |
| Chain | Residue |
| A | CYS2 |
| A | ARG95 |
| A | TRP96 |
| A | THR98 |
| A | HIS99 |
| A | HIS108 |
| A | HIS122 |
| A | ASN123 |
| A | GLY124 |
| A | ASP148 |
| A | THR149 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue G6Q B 701 |
| Chain | Residue |
| A | HIS577 |
| B | CYS374 |
| B | GLY375 |
| B | THR376 |
| B | SER377 |
| B | SER421 |
| B | GLN422 |
| B | SER423 |
| B | THR426 |
| B | ALA473 |
| B | SER474 |
| B | LYS558 |
| B | GLU561 |
| B | HOH807 |
| B | HOH825 |
| B | HOH830 |
| B | HOH831 |
| B | HOH836 |
| B | HOH846 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: For GATase activity => ECO:0000250|UniProtKB:P14742 |
| Chain | Residue | Details |
| A | CYS2 | |
| B | CYS2 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19059404, ECO:0007744|PDB:2V4M, ECO:0007744|PDB:2ZJ3, ECO:0007744|PDB:2ZJ4 |
| Chain | Residue | Details |
| A | THR376 | |
| A | SER421 | |
| A | THR426 | |
| A | HIS577 | |
| B | THR376 | |
| B | SER421 | |
| B | THR426 | |
| B | HIS577 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER103 | |
| B | SER103 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER261 | |
| B | SER261 |
