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 PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue IMP A 500 |
| Chain | Residue |
| A | ALA47 |
| A | GLY338 |
| A | GLY359 |
| A | SER360 |
| A | TYR383 |
| A | GLY385 |
| A | MET386 |
| A | GLY387 |
| A | GLU411 |
| A | GLY412 |
| A | 8LA501 |
| A | MET49 |
| A | HOH601 |
| A | HOH606 |
| A | HOH607 |
| A | HOH615 |
| A | HOH628 |
| A | ASN275 |
| A | GLY300 |
| A | SER301 |
| A | ILE302 |
| A | CYS303 |
| A | ASP336 |
| A | GLY337 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue 8LA A 501 |
| Chain | Residue |
| A | THR247 |
| A | ALA248 |
| A | HIS249 |
| A | SER252 |
| A | GLY254 |
| A | VAL255 |
| A | THR305 |
| A | MET386 |
| A | GLY387 |
| A | MET392 |
| A | VAL409 |
| A | GLU411 |
| A | IMP500 |
| C | LEU24 |
| C | PRO25 |
| C | SER436 |
| C | GLY439 |
| C | TYR440 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue K A 502 |
| Chain | Residue |
| A | GLY298 |
| A | GLY300 |
| A | CYS303 |
| C | GLU465 |
| C | SER466 |
| C | HIS467 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | binding site for residue IMP B 501 |
| Chain | Residue |
| B | ALA47 |
| B | MET49 |
| B | ASN275 |
| B | GLY300 |
| B | SER301 |
| B | ILE302 |
| B | CYS303 |
| B | ASP336 |
| B | GLY337 |
| B | GLY338 |
| B | MET358 |
| B | GLY359 |
| B | SER360 |
| B | TYR383 |
| B | GLY385 |
| B | MET386 |
| B | GLY387 |
| B | GLU411 |
| B | GLY412 |
| B | 8LA502 |
| B | HOH604 |
| B | HOH626 |
| B | HOH627 |
| B | HOH643 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue 8LA B 502 |
| Chain | Residue |
| A | VAL23 |
| A | LEU24 |
| A | PRO25 |
| A | SER436 |
| A | GLY439 |
| A | TYR440 |
| B | THR247 |
| B | ALA248 |
| B | HIS249 |
| B | SER252 |
| B | GLY254 |
| B | VAL255 |
| B | THR305 |
| B | MET386 |
| B | GLY387 |
| B | VAL409 |
| B | GLU411 |
| B | IMP501 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MPD B 503 |
| Chain | Residue |
| B | LYS6 |
| B | ALA277 |
| B | PRO279 |
| B | ASP321 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue K B 504 |
| Chain | Residue |
| D | CYS303 |
| B | GLU465 |
| B | SER466 |
| B | HIS467 |
| D | GLY298 |
| D | GLY300 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue FMT C 501 |
| Chain | Residue |
| A | SER460 |
| A | HOH632 |
| B | SER460 |
| C | SER460 |
| D | SER460 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | binding site for residue IMP C 502 |
| Chain | Residue |
| C | ALA47 |
| C | MET49 |
| C | ASN275 |
| C | GLY300 |
| C | SER301 |
| C | ILE302 |
| C | CYS303 |
| C | ASP336 |
| C | GLY337 |
| C | GLY338 |
| C | MET358 |
| C | GLY359 |
| C | SER360 |
| C | TYR383 |
| C | GLY385 |
| C | MET386 |
| C | GLY387 |
| C | GLU411 |
| C | GLY412 |
| C | 8LA503 |
| C | HOH618 |
| C | HOH627 |
| C | HOH640 |
| C | HOH642 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for residue 8LA C 503 |
| Chain | Residue |
| C | THR247 |
| C | ALA248 |
| C | HIS249 |
| C | SER252 |
| C | GLY254 |
| C | VAL255 |
| C | THR305 |
| C | MET386 |
| C | GLY387 |
| C | MET392 |
| C | GLU411 |
| C | IMP502 |
| D | LEU24 |
| D | PRO25 |
| D | SER436 |
| D | GLY439 |
| D | TYR440 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 504 |
| Chain | Residue |
| C | ALA277 |
| C | THR278 |
| C | ASP321 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue K D 501 |
| Chain | Residue |
| C | GLY298 |
| C | GLY300 |
| C | CYS303 |
| D | GLU465 |
| D | SER466 |
| D | HIS467 |
| site_id | AD4 |
| Number of Residues | 26 |
| Details | binding site for residue IMP D 502 |
| Chain | Residue |
| D | ALA47 |
| D | MET49 |
| D | ASN275 |
| D | GLY300 |
| D | SER301 |
| D | ILE302 |
| D | CYS303 |
| D | ASP336 |
| D | GLY337 |
| D | GLY338 |
| D | MET357 |
| D | MET358 |
| D | GLY359 |
| D | SER360 |
| D | TYR383 |
| D | GLY385 |
| D | MET386 |
| D | GLY387 |
| D | GLU411 |
| D | GLY412 |
| D | 8LA503 |
| D | HOH609 |
| D | HOH620 |
| D | HOH629 |
| D | HOH638 |
| D | HOH651 |
| site_id | AD5 |
| Number of Residues | 18 |
| Details | binding site for residue 8LA D 503 |
| Chain | Residue |
| B | VAL23 |
| B | LEU24 |
| B | PRO25 |
| B | SER436 |
| B | GLY439 |
| B | TYR440 |
| D | THR247 |
| D | ALA248 |
| D | HIS249 |
| D | SER252 |
| D | GLY254 |
| D | VAL255 |
| D | THR305 |
| D | MET386 |
| D | GLY387 |
| D | VAL409 |
| D | GLU411 |
| D | IMP502 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue MPD D 504 |
| Chain | Residue |
| D | LYS6 |
| D | ALA277 |
| D | ASP321 |
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 | VAL293-THR305 | |
