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 | 23 |
| Details | binding site for residue IMP A 500 |
| Chain | Residue |
| A | ALA47 |
| A | MET358 |
| A | GLY359 |
| A | SER360 |
| A | TYR383 |
| A | GLY385 |
| A | MET386 |
| A | GLY387 |
| A | GLU411 |
| A | GLY412 |
| A | 8L1501 |
| A | ASN275 |
| A | HOH608 |
| A | HOH610 |
| A | HOH613 |
| A | HOH615 |
| A | GLY300 |
| A | SER301 |
| A | ILE302 |
| A | CYS303 |
| A | ASP336 |
| A | GLY337 |
| A | GLY338 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue 8L1 A 501 |
| Chain | Residue |
| A | VAL224 |
| A | ALA248 |
| A | HIS249 |
| A | SER252 |
| A | THR305 |
| A | GLY387 |
| A | VAL409 |
| A | GLU411 |
| A | IMP500 |
| 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 | GLU465 |
| A | SER466 |
| A | HIS467 |
| B | GLY298 |
| B | GLY300 |
| B | CYS303 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue IMP B 501 |
| Chain | Residue |
| B | ALA47 |
| 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 | 8L1502 |
| B | HOH605 |
| B | HOH619 |
| B | HOH622 |
| B | HOH635 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue 8L1 B 502 |
| Chain | Residue |
| A | PRO25 |
| A | SER436 |
| A | GLY439 |
| A | TYR440 |
| B | VAL224 |
| B | ALA248 |
| B | THR305 |
| B | GLY387 |
| B | GLU411 |
| B | IMP501 |
| B | HOH606 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue K B 503 |
| Chain | Residue |
| B | GLU465 |
| B | SER466 |
| B | HIS467 |
| D | GLY298 |
| D | GLY300 |
| D | CYS303 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | TYR450 |
| B | GLU451 |
| B | ALA453 |
| B | HOH623 |
| D | ARG3 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | binding site for residue IMP C 500 |
| Chain | Residue |
| C | SER360 |
| C | TYR383 |
| C | GLY385 |
| C | MET386 |
| C | GLY387 |
| C | GLU411 |
| C | GLY412 |
| C | 8L1501 |
| C | HOH619 |
| C | HOH626 |
| C | ALA47 |
| C | MET49 |
| C | ASN275 |
| C | GLY300 |
| C | SER301 |
| C | ILE302 |
| C | CYS303 |
| C | ASP336 |
| C | GLY338 |
| C | MET357 |
| C | MET358 |
| C | GLY359 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue 8L1 C 501 |
| Chain | Residue |
| C | VAL224 |
| C | ALA248 |
| C | HIS249 |
| C | SER252 |
| C | THR305 |
| C | GLY387 |
| C | MET392 |
| C | GLU411 |
| C | IMP500 |
| D | PRO25 |
| D | SER436 |
| D | GLY439 |
| D | TYR440 |
| site_id | AD1 |
| Number of Residues | 22 |
| Details | binding site for residue IMP D 500 |
| Chain | Residue |
| D | ALA47 |
| D | MET49 |
| D | GLY300 |
| D | SER301 |
| D | ILE302 |
| D | CYS303 |
| D | ASP336 |
| D | GLY337 |
| D | GLY338 |
| D | MET358 |
| D | GLY359 |
| D | SER360 |
| D | TYR383 |
| D | GLY385 |
| D | MET386 |
| D | GLY387 |
| D | GLU411 |
| D | GLY412 |
| D | 8L1501 |
| D | HOH612 |
| D | HOH621 |
| D | HOH628 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for residue 8L1 D 501 |
| Chain | Residue |
| B | SER436 |
| B | GLY439 |
| B | TYR440 |
| D | VAL224 |
| D | THR247 |
| D | ALA248 |
| D | HIS249 |
| D | SER252 |
| D | THR305 |
| D | MET386 |
| D | GLY387 |
| D | GLU411 |
| D | IMP500 |
| D | HOH627 |
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 | |
