6RUL
Crystal structure of GFP-LAMA-F98 - a GFP enhancer nanobody with cpDHFR insertion and TMP and NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005542 | molecular_function | folic acid binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0009257 | biological_process | 10-formyltetrahydrofolate biosynthetic process |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031427 | biological_process | response to methotrexate |
| A | 0046452 | biological_process | dihydrofolate metabolic process |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046655 | biological_process | folic acid metabolic process |
| A | 0046656 | biological_process | folic acid biosynthetic process |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051870 | molecular_function | methotrexate binding |
| A | 0051871 | molecular_function | dihydrofolic acid binding |
| A | 0070401 | molecular_function | NADP+ binding |
| A | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue TOP A 301 |
| Chain | Residue |
| A | ASP102 |
| A | NDP302 |
| A | HOH411 |
| A | HOH424 |
| A | PHE106 |
| A | ILE169 |
| A | TYR175 |
| A | THR188 |
| A | ILE244 |
| A | ALA245 |
| A | ALA246 |
| A | MET259 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | binding site for residue NDP A 302 |
| Chain | Residue |
| A | GLY118 |
| A | ARG119 |
| A | HIS120 |
| A | THR121 |
| A | SER124 |
| A | LEU137 |
| A | SER138 |
| A | SER139 |
| A | GLN140 |
| A | LYS151 |
| A | ILE169 |
| A | GLY171 |
| A | GLY172 |
| A | ARG173 |
| A | VAL174 |
| A | TYR175 |
| A | GLN177 |
| A | THR198 |
| A | ALA245 |
| A | ALA246 |
| A | ILE253 |
| A | GLY254 |
| A | ASN257 |
| A | ALA258 |
| A | TRP261 |
| A | TOP301 |
| A | HOH412 |
| A | HOH428 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 303 |
| Chain | Residue |
| A | ARG45 |
| A | TYR91 |
| A | GLU123 |
| A | GLU256 |
| A | TRP265 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:9012674 |
| Chain | Residue | Details |
| A | ILE244 | |
| A | ASP102 | |
| A | ARG127 | |
| A | ARG132 | |
| A | THR188 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19374017 |
| Chain | Residue | Details |
| A | ALA246 | |
| A | VAL252 | |
| A | HIS120 | |
| A | SER138 | |
| A | LYS151 | |
| A | GLY170 |
