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 | 20 |
| Details | BINDING SITE FOR RESIDUE IMP A 501 |
| Chain | Residue |
| A | ALA49 |
| A | GLY363 |
| A | SER364 |
| A | TYR387 |
| A | MET390 |
| A | GLU417 |
| A | HOH626 |
| A | HOH697 |
| A | HOH733 |
| A | HOH786 |
| A | HOH821 |
| A | MET51 |
| A | HOH825 |
| A | GLY304 |
| A | SER305 |
| A | ILE306 |
| A | ASP340 |
| A | GLY342 |
| A | MET361 |
| A | VAL362 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE IMP B 501 |
| Chain | Residue |
| B | ALA49 |
| B | MET51 |
| B | ASN279 |
| B | GLY304 |
| B | SER305 |
| B | ILE306 |
| B | ASP340 |
| B | GLY341 |
| B | GLY342 |
| B | MET361 |
| B | VAL362 |
| B | GLY363 |
| B | SER364 |
| B | TYR387 |
| B | MET390 |
| B | GLU417 |
| B | HOH612 |
| B | HOH626 |
| B | HOH677 |
| B | HOH725 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 501 |
| Chain | Residue |
| B | GLY302 |
| B | GLY304 |
| B | CYS307 |
| C | GLU471 |
| C | SER472 |
| C | HIS473 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE IMP C 502 |
| Chain | Residue |
| C | ALA49 |
| C | MET51 |
| C | GLY304 |
| C | SER305 |
| C | ILE306 |
| C | CYS307 |
| C | ASP340 |
| C | GLY342 |
| C | MET361 |
| C | VAL362 |
| C | GLY363 |
| C | SER364 |
| C | TYR387 |
| C | GLY389 |
| C | MET390 |
| C | GLU417 |
| C | HOH620 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 503 |
| Chain | Residue |
| B | GLU471 |
| B | SER472 |
| B | HIS473 |
| C | GLY302 |
| C | GLY304 |
| C | CYS307 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K D 501 |
| Chain | Residue |
| A | GLY302 |
| A | GLY304 |
| A | CYS307 |
| D | GLU471 |
| D | SER472 |
| D | HIS473 |
| D | HIS475 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE IMP D 502 |
| Chain | Residue |
| D | ALA49 |
| D | MET51 |
| D | GLY304 |
| D | SER305 |
| D | ILE306 |
| D | CYS307 |
| D | ASP340 |
| D | GLY341 |
| D | GLY342 |
| D | MET361 |
| D | VAL362 |
| D | GLY363 |
| D | SER364 |
| D | TYR387 |
| D | GLY389 |
| D | MET390 |
| D | GLU417 |
| D | HOH602 |
| D | HOH622 |
| D | HOH669 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D 503 |
| Chain | Residue |
| D | GLY302 |
| D | GLY304 |
| D | CYS307 |
| A | GLU471 |
| A | SER472 |
| A | HIS473 |
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 | VAL297-THR309 | |
