6R4E
Crystal structure of human GFAT-1 in complex with Glucose-6-Phosphate and L-Glu
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 | 16 |
| Details | binding site for residue G6Q A 701 |
| Chain | Residue |
| A | CYS374 |
| A | LYS558 |
| A | GLU561 |
| A | HOH802 |
| A | HOH806 |
| A | HOH815 |
| A | HOH826 |
| B | HIS577 |
| A | GLY375 |
| A | THR376 |
| A | SER377 |
| A | SER421 |
| A | GLN422 |
| A | SER423 |
| A | THR426 |
| A | SER474 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue GLU A 702 |
| Chain | Residue |
| A | CYS2 |
| A | ARG95 |
| A | TRP96 |
| A | THR98 |
| A | HIS99 |
| A | HIS108 |
| A | ASN123 |
| A | GLY124 |
| A | ASP148 |
| A | THR149 |
| site_id | AC3 |
| Number of Residues | 15 |
| 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 | HOH801 |
| B | HOH806 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 278 |
| Details | Domain: {"description":"SIS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00797","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 282 |
| Details | Domain: {"description":"SIS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00797","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"For GATase activity","evidences":[{"source":"UniProtKB","id":"P14742","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19059404","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZJ4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
