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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE IMP A 501 |
| Chain | Residue |
| A | ALA49 |
| A | GLY363 |
| A | SER364 |
| A | TYR387 |
| A | GLY389 |
| A | MET390 |
| A | GLY391 |
| A | GLU417 |
| A | GLY418 |
| A | NAJ502 |
| A | HOH609 |
| A | MET51 |
| A | HOH615 |
| A | HOH624 |
| A | HOH683 |
| A | GLY304 |
| A | SER305 |
| A | ILE306 |
| A | CYS307 |
| A | ASP340 |
| A | GLY341 |
| A | GLY342 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAJ A 502 |
| Chain | Residue |
| A | LEU26 |
| A | PRO27 |
| A | LYS74 |
| A | ASP250 |
| A | SER251 |
| A | SER252 |
| A | SER256 |
| A | GLY300 |
| A | ILE301 |
| A | GLY302 |
| A | CYS307 |
| A | THR309 |
| A | MET390 |
| A | GLY391 |
| A | GLU417 |
| A | SER442 |
| A | GLY445 |
| A | LEU446 |
| A | IMP501 |
| A | HOH682 |
| A | HOH695 |
| A | HOH702 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 503 |
| Chain | Residue |
| A | GLY302 |
| A | GLY304 |
| A | CYS307 |
| A | GLU471 |
| A | SER472 |
| A | HIS473 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE IMP B 501 |
| Chain | Residue |
| B | ALA49 |
| B | MET51 |
| B | GLY304 |
| B | SER305 |
| B | ILE306 |
| B | CYS307 |
| B | THR309 |
| B | ASP340 |
| B | GLY342 |
| B | MET361 |
| B | GLY363 |
| B | SER364 |
| B | TYR387 |
| B | GLY389 |
| B | MET390 |
| B | GLY391 |
| B | GLU417 |
| B | GLY418 |
| B | NAJ502 |
| B | HOH603 |
| B | HOH609 |
| B | HOH625 |
| B | HOH649 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAJ B 502 |
| Chain | Residue |
| B | ASP250 |
| B | SER251 |
| B | SER252 |
| B | SER256 |
| B | ASN279 |
| B | GLY300 |
| B | ILE301 |
| B | GLY302 |
| B | CYS307 |
| B | THR309 |
| B | MET390 |
| B | GLY391 |
| B | SER442 |
| B | GLY445 |
| B | LEU446 |
| B | IMP501 |
| B | HOH629 |
| B | HOH672 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 503 |
| Chain | Residue |
| B | GLY302 |
| B | GLY304 |
| B | CYS307 |
| B | GLU471 |
| B | SER472 |
| B | 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 | |
4QNE
