5CHE
Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its regulatory proteins
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008883 | molecular_function | glutamyl-tRNA reductase activity |
| A | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| A | 0050661 | molecular_function | NADP binding |
| B | 0008883 | molecular_function | glutamyl-tRNA reductase activity |
| B | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| B | 0050661 | molecular_function | NADP binding |
| E | 0015995 | biological_process | chlorophyll biosynthetic process |
| E | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| F | 0015995 | biological_process | chlorophyll biosynthetic process |
| F | 0033014 | biological_process | tetrapyrrole biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS00747 |
| Number of Residues | 24 |
| Details | GLUTR Glutamyl-tRNA reductase signature. HIfeVSAGLDSlVLGEgQILAQVK |
| Chain | Residue | Details |
| A | HIS193-LYS216 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS144 | |
| B | CYS144 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | THR143 | |
| B | GLY285 | |
| A | SER203 | |
| A | GLU208 | |
| A | GLN214 | |
| A | GLY285 | |
| B | THR143 | |
| B | SER203 | |
| B | GLU208 | |
| B | GLN214 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Important for activity => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS193 | |
| B | HIS193 |
