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 | 6 |
| Details | BINDING SITE FOR RESIDUE K A 981 |
| Chain | Residue |
| A | GLU485 |
| A | GLY486 |
| A | GLY487 |
| D | GLY314 |
| D | GLY316 |
| D | CYS319 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 982 |
| Chain | Residue |
| B | GLU485 |
| B | GLY486 |
| B | GLY487 |
| A | GLY314 |
| A | GLY316 |
| A | CYS319 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D 983 |
| Chain | Residue |
| C | GLY314 |
| C | GLY316 |
| C | CYS319 |
| D | GLU485 |
| D | GLY486 |
| D | GLY487 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 984 |
| Chain | Residue |
| C | ASP264 |
| C | PHE266 |
| D | GLY20 |
| D | SER22 |
| D | ASN460 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 985 |
| Chain | Residue |
| B | GLY314 |
| B | GLY316 |
| B | CYS319 |
| C | GLU485 |
| C | GLY486 |
| C | GLY487 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 986 |
| Chain | Residue |
| B | ASP264 |
| B | PHE266 |
| C | GLY20 |
| C | SER22 |
| C | ASN460 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 987 |
| Chain | Residue |
| A | ASP264 |
| A | PHE266 |
| B | GLY20 |
| B | SER22 |
| B | ASN460 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 988 |
| Chain | Residue |
| A | GLY20 |
| A | SER22 |
| A | ASN460 |
| D | ASP264 |
| D | PHE266 |
| site_id | AC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE MZP A 971 |
| Chain | Residue |
| A | ALA57 |
| A | MET59 |
| A | GLY316 |
| A | SER317 |
| A | ILE318 |
| A | CYS319 |
| A | ASP358 |
| A | GLY359 |
| A | GLY360 |
| A | MET379 |
| A | LEU380 |
| A | GLY381 |
| A | ARG382 |
| A | TYR405 |
| A | GLY407 |
| A | GLU408 |
| A | GLY409 |
| A | ARG418 |
| A | TYR419 |
| A | GLU431 |
| A | GLY432 |
| A | HOH1004 |
| A | HOH1010 |
| A | HOH1012 |
| A | HOH1028 |
| A | HOH1029 |
| A | HOH1053 |
| site_id | BC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE MZP B 972 |
| Chain | Residue |
| B | HOH1124 |
| B | ALA57 |
| B | MET59 |
| B | GLY316 |
| B | SER317 |
| B | ILE318 |
| B | CYS319 |
| B | ASP358 |
| B | GLY359 |
| B | GLY360 |
| B | MET379 |
| B | LEU380 |
| B | GLY381 |
| B | ARG382 |
| B | TYR405 |
| B | GLY407 |
| B | GLU408 |
| B | GLY409 |
| B | ARG418 |
| B | TYR419 |
| B | GLU431 |
| B | GLY432 |
| B | HOH997 |
| B | HOH1000 |
| B | HOH1008 |
| B | HOH1023 |
| B | HOH1036 |
| B | HOH1041 |
| B | HOH1046 |
| site_id | BC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE MZP C 973 |
| Chain | Residue |
| C | ALA57 |
| C | MET59 |
| C | GLY316 |
| C | SER317 |
| C | ILE318 |
| C | CYS319 |
| C | ASP358 |
| C | GLY359 |
| C | GLY360 |
| C | MET379 |
| C | LEU380 |
| C | GLY381 |
| C | ARG382 |
| C | TYR405 |
| C | GLY407 |
| C | GLU408 |
| C | GLY409 |
| C | ARG418 |
| C | TYR419 |
| C | GLU431 |
| C | GLY432 |
| C | HOH998 |
| C | HOH1005 |
| C | HOH1007 |
| C | HOH1014 |
| C | HOH1015 |
| C | HOH1039 |
| site_id | BC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE MZP D 974 |
| Chain | Residue |
| D | ALA57 |
| D | MET59 |
| D | GLY316 |
| D | SER317 |
| D | ILE318 |
| D | CYS319 |
| D | ASP358 |
| D | GLY359 |
| D | GLY360 |
| D | MET379 |
| D | LEU380 |
| D | GLY381 |
| D | ARG382 |
| D | TYR405 |
| D | GLY407 |
| D | GLU408 |
| D | GLY409 |
| D | ARG418 |
| D | TYR419 |
| D | GLU431 |
| D | GLY432 |
| D | HOH1001 |
| D | HOH1005 |
| D | HOH1017 |
| D | HOH1022 |
| D | HOH1037 |
| D | HOH1051 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TRS B 991 |
| Chain | Residue |
| B | ASP364 |
| B | TYR383 |
| B | ARG386 |
| B | ASN446 |
| B | ALA449 |
| B | SER450 |
| B | LYS453 |
| B | HOH1192 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS C 992 |
| Chain | Residue |
| B | ALA2 |
| C | VAL339 |
| C | ASN343 |
| C | HOH997 |
| C | HOH999 |
| C | HOH1051 |
| C | HOH1063 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS A 993 |
| Chain | Residue |
| A | VAL339 |
| A | ALA340 |
| A | ASN343 |
| A | HOH1001 |
| A | HOH1018 |
| A | HOH1040 |
| A | HOH1093 |
| A | HOH1097 |
| D | ALA2 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS B 994 |
| Chain | Residue |
| A | ALA2 |
| A | HOH1008 |
| B | VAL339 |
| B | ASN343 |
| B | HOH999 |
| B | HOH1075 |
| B | HOH1077 |
| B | HOH1176 |
| B | HOH1233 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS D 995 |
| Chain | Residue |
| C | ALA2 |
| C | HOH1040 |
| D | VAL339 |
| D | ASN343 |
| D | HOH998 |
| D | HOH1011 |
| D | HOH1085 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS A 996 |
| Chain | Residue |
| A | TYR15 |
| A | ILE336 |
| A | LEU477 |
| A | HOH1062 |
| D | HOH999 |
| D | HOH1069 |
| D | HOH1084 |
Functional Information from PROSITE/UniProt
| site_id | PS00487 |
| Number of Residues | 13 |
| Details | IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKIGIGgGSICiT |
| Chain | Residue | Details |
| A | ILE309-THR321 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | CYS319 | |
| B | CYS319 | |
| C | CYS319 | |
| D | CYS319 | |
| Chain | Residue | Details |
| A | ARG418 | |
| B | ARG418 | |
| C | ARG418 | |
| D | ARG418 | |
| Chain | Residue | Details |
| A | GLY20 | |
| B | GLY316 | |
| B | CYS319 | |
| B | ASN460 | |
| C | GLY20 | |
| C | SER22 | |
| C | GLY314 | |
| C | GLY316 | |
| C | CYS319 | |
| C | ASN460 | |
| D | GLY20 | |
| A | SER22 | |
| D | SER22 | |
| D | GLY314 | |
| D | GLY316 | |
| D | CYS319 | |
| D | ASN460 | |
| A | GLY314 | |
| A | GLY316 | |
| A | CYS319 | |
| A | ASN460 | |
| B | GLY20 | |
| B | SER22 | |
| B | GLY314 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP261 | |
| B | SER317 | |
| B | ASP358 | |
| B | GLY381 | |
| B | TYR405 | |
| B | GLU431 | |
| C | ASP261 | |
| C | GLY312 | |
| C | SER317 | |
| C | ASP358 | |
| C | GLY381 | |
| A | GLY312 | |
| C | TYR405 | |
| C | GLU431 | |
| D | ASP261 | |
| D | GLY312 | |
| D | SER317 | |
| D | ASP358 | |
| D | GLY381 | |
| D | TYR405 | |
| D | GLU431 | |
| A | SER317 | |
| A | ASP358 | |
| A | GLY381 | |
| A | TYR405 | |
| A | GLU431 | |
| B | ASP261 | |
| B | GLY312 | |
| Chain | Residue | Details |
| A | ASP264 | |
| B | GLY487 | |
| C | ASP264 | |
| C | PHE266 | |
| C | GLU485 | |
| C | GLY486 | |
| C | GLY487 | |
| D | ASP264 | |
| D | PHE266 | |
| D | GLU485 | |
| D | GLY486 | |
| A | PHE266 | |
| D | GLY487 | |
| A | GLU485 | |
| A | GLY486 | |
| A | GLY487 | |
| B | ASP264 | |
| B | PHE266 | |
| B | GLU485 | |
| B | GLY486 | |
