7NDL
Crystal structure of human GFAT-1 S205D
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 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 |