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 | 25 |
| Details | BINDING SITE FOR RESIDUE IMP A 500 |
| Chain | Residue |
| A | ALA49 |
| A | GLY343 |
| A | MET362 |
| A | GLY364 |
| A | SER365 |
| A | TYR388 |
| A | GLY390 |
| A | MET391 |
| A | GLY392 |
| A | GLU416 |
| A | GLY417 |
| A | MET51 |
| A | 2EY501 |
| A | HOH606 |
| A | HOH613 |
| A | HOH624 |
| A | HOH628 |
| A | HOH707 |
| A | ASN280 |
| A | GLY305 |
| A | SER306 |
| A | ILE307 |
| A | CYS308 |
| A | ASP341 |
| A | GLY342 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 2EY A 501 |
| Chain | Residue |
| A | ALA253 |
| A | THR310 |
| A | MET391 |
| A | GLY392 |
| A | MET397 |
| A | LEU413 |
| A | VAL414 |
| A | GLU416 |
| A | GLY444 |
| A | TYR445 |
| A | IMP500 |
| A | HOH772 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 502 |
| Chain | Residue |
| A | PHE6 |
| A | GLU9 |
| A | THR322 |
| A | HOH627 |
| A | HOH792 |
| A | HOH809 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | GLU38 |
| A | SER39 |
| A | PRO272 |
| A | SER273 |
| A | ASN296 |
| A | HOH770 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE IMP B 500 |
| Chain | Residue |
| B | ALA49 |
| B | MET51 |
| B | ASN280 |
| B | GLY305 |
| B | SER306 |
| B | ILE307 |
| B | CYS308 |
| B | ASP341 |
| B | GLY342 |
| B | GLY343 |
| B | MET362 |
| B | GLY364 |
| B | SER365 |
| B | TYR388 |
| B | GLY390 |
| B | MET391 |
| B | GLY392 |
| B | GLU416 |
| B | GLY417 |
| B | 2EY501 |
| B | HOH604 |
| B | HOH610 |
| B | HOH627 |
| B | HOH640 |
| B | HOH650 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 2EY B 501 |
| Chain | Residue |
| B | MET391 |
| B | GLY392 |
| B | MET397 |
| B | LEU413 |
| B | VAL414 |
| B | GLU416 |
| B | GLY444 |
| B | TYR445 |
| B | IMP500 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| B | GLU9 |
| B | THR322 |
| B | HOH646 |
| B | HOH808 |
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 | VAL298-THR310 | |
