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 501 |
| 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 | Q21502 |
| A | HOH606 |
| A | HOH638 |
| A | HOH653 |
| A | HOH654 |
| A | ASN280 |
| A | GLY305 |
| A | SER306 |
| A | ILE307 |
| A | CYS308 |
| A | ASP341 |
| A | GLY342 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE Q21 A 502 |
| Chain | Residue |
| A | ALA253 |
| A | SER257 |
| A | MET391 |
| A | GLY392 |
| A | GLU416 |
| A | IMP501 |
| A | HOH609 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | VAL30 |
| A | SER31 |
| A | VAL32 |
| A | LYS33 |
| A | ARG440 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | ALA62 |
| A | ARG65 |
| A | GLU372 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 505 |
| Chain | Residue |
| A | ALA64 |
| A | GLY67 |
| A | GLY68 |
| A | LEU222 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 506 |
| Chain | Residue |
| A | SER273 |
| A | ASN275 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 507 |
| Chain | Residue |
| A | TYR346 |
| A | SER347 |
| D | VAL312 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE IMP B 501 |
| Chain | Residue |
| B | ALA49 |
| B | MET51 |
| B | ASN280 |
| B | GLY305 |
| B | SER306 |
| B | ILE307 |
| B | CYS308 |
| B | ASP341 |
| B | GLY343 |
| B | LEU363 |
| B | GLY364 |
| B | SER365 |
| B | TYR388 |
| B | GLY390 |
| B | MET391 |
| B | GLY392 |
| B | GLU416 |
| B | GLY417 |
| B | Q21502 |
| B | HOH609 |
| B | HOH613 |
| B | HOH619 |
| B | HOH637 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE Q21 B 502 |
| Chain | Residue |
| B | ALA253 |
| B | SER257 |
| B | MET391 |
| B | GLY392 |
| B | MET397 |
| B | LEU413 |
| B | GLU416 |
| B | IMP501 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 503 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT B 504 |
| Chain | Residue |
| B | ASN275 |
| B | ASN296 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 505 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT B 506 |
| Chain | Residue |
| B | TYR424 |
| B | LYS425 |
| B | GLY426 |
| B | HOH656 |
| B | HOH676 |
| site_id | BC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE Q21 B 507 |
| Chain | Residue |
| C | LEU413 |
| C | GLU416 |
| C | IMP501 |
| B | SER23 |
| B | VAL25 |
| B | PRO27 |
| B | ALA441 |
| B | GLY444 |
| B | TYR445 |
| C | ALA253 |
| C | SER257 |
| C | MET391 |
| C | GLY392 |
| site_id | BC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE IMP C 501 |
| Chain | Residue |
| B | Q21507 |
| C | ALA49 |
| C | MET51 |
| C | ASN280 |
| C | GLY305 |
| C | SER306 |
| C | CYS308 |
| C | ASP341 |
| C | GLY343 |
| C | GLY364 |
| C | SER365 |
| C | TYR388 |
| C | GLY390 |
| C | MET391 |
| C | GLY392 |
| C | GLU416 |
| C | GLY417 |
| C | HOH601 |
| C | HOH608 |
| C | HOH621 |
| C | HOH660 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT C 502 |
| Chain | Residue |
| C | GLN41 |
| C | LEU42 |
| C | ASN43 |
| C | HOH646 |
| C | HOH649 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY C 503 |
| Chain | Residue |
| C | LEU11 |
| C | THR322 |
| C | TYR325 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 501 |
| Chain | Residue |
| A | GLY437 |
| D | LYS412 |
| D | LEU413 |
| D | VAL414 |
| D | HOH644 |
| site_id | CC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE IMP D 502 |
| Chain | Residue |
| D | ALA49 |
| D | MET51 |
| D | ASN280 |
| D | SER306 |
| D | ILE307 |
| D | CYS308 |
| D | ASP341 |
| D | GLY342 |
| D | GLY343 |
| D | LEU363 |
| D | GLY364 |
| D | SER365 |
| D | TYR388 |
| D | GLY390 |
| D | MET391 |
| D | GLY392 |
| D | GLU416 |
| D | GLY417 |
| D | Q21503 |
| D | HOH601 |
| D | HOH606 |
| D | HOH609 |
| D | HOH635 |
| site_id | CC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE Q21 D 503 |
| Chain | Residue |
| A | SER23 |
| A | LEU26 |
| A | ALA441 |
| A | TYR445 |
| D | ALA253 |
| D | SER257 |
| D | MET391 |
| D | GLY392 |
| D | LEU413 |
| D | VAL414 |
| D | GLU416 |
| D | IMP502 |
| D | HOH621 |
| site_id | CC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT D 504 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT D 506 |
| Chain | Residue |
| D | ARG268 |
| D | SER273 |
| D | ASN275 |
| D | ASN296 |
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 | |
