7QBJ
bacterial IMPDH chimera
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003938 | molecular_function | IMP dehydrogenase activity |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003938 | molecular_function | IMP dehydrogenase activity |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003938 | molecular_function | IMP dehydrogenase activity |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003938 | molecular_function | IMP dehydrogenase activity |
| D | 0006164 | biological_process | purine nucleotide biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00487 |
| Number of Residues | 13 |
| Details | IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT |
| Chain | Residue | Details |
| A | VAL294-THR306 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_01964 |
| Chain | Residue | Details |
| A | CYS304 | |
| B | CYS304 | |
| C | CYS304 | |
| D | CYS304 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01964 |
| Chain | Residue | Details |
| A | ARG400 | |
| B | ARG400 | |
| C | ARG400 | |
| D | ARG400 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01964 |
| Chain | Residue | Details |
| A | ASP247 | |
| A | HIS470 | |
| B | ASP247 | |
| B | GLY297 | |
| B | SER302 | |
| B | ASP337 | |
| B | GLY360 | |
| B | TYR384 | |
| B | GLU414 | |
| B | GLU468 | |
| B | SER469 | |
| A | GLY297 | |
| B | HIS470 | |
| C | ASP247 | |
| C | GLY297 | |
| C | SER302 | |
| C | ASP337 | |
| C | GLY360 | |
| C | TYR384 | |
| C | GLU414 | |
| C | GLU468 | |
| C | SER469 | |
| A | SER302 | |
| C | HIS470 | |
| D | ASP247 | |
| D | GLY297 | |
| D | SER302 | |
| D | ASP337 | |
| D | GLY360 | |
| D | TYR384 | |
| D | GLU414 | |
| D | GLU468 | |
| D | SER469 | |
| A | ASP337 | |
| D | HIS470 | |
| A | GLY360 | |
| A | TYR384 | |
| A | GLU414 | |
| A | GLU468 | |
| A | SER469 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01964 |
| Chain | Residue | Details |
| A | GLY299 | |
| D | GLY299 | |
| D | GLY301 | |
| D | CYS304 | |
| A | GLY301 | |
| A | CYS304 | |
| B | GLY299 | |
| B | GLY301 | |
| B | CYS304 | |
| C | GLY299 | |
| C | GLY301 | |
| C | CYS304 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS266 | |
| A | LYS427 | |
| B | LYS266 | |
| B | LYS427 | |
| C | LYS266 | |
| C | LYS427 | |
| D | LYS266 | |
| D | LYS427 |
