2CU0
Crystal structure of inosine-5'-monophosphate dehydrogenase from Pyrococcus horikoshii OT3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003938 | molecular_function | IMP dehydrogenase activity |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006177 | biological_process | GMP biosynthetic process |
| A | 0006183 | biological_process | GTP biosynthetic process |
| A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003938 | molecular_function | IMP dehydrogenase activity |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006177 | biological_process | GMP biosynthetic process |
| B | 0006183 | biological_process | GTP biosynthetic process |
| B | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE XMP A 1001 |
| Chain | Residue |
| A | MET55 |
| A | MET355 |
| A | GLY357 |
| A | ASN358 |
| A | TYR381 |
| A | GLY383 |
| A | MET384 |
| A | GLY385 |
| A | GLU412 |
| A | GLY413 |
| A | HOH1005 |
| A | GLY298 |
| A | HOH1020 |
| A | HOH1024 |
| A | HOH1030 |
| A | HOH1049 |
| A | HOH1118 |
| A | SER299 |
| A | ILE300 |
| A | CYS301 |
| A | THR303 |
| A | ASP334 |
| A | GLY335 |
| A | GLY336 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE XMP B 1002 |
| Chain | Residue |
| B | ALA53 |
| B | MET55 |
| B | GLY298 |
| B | SER299 |
| B | ILE300 |
| B | CYS301 |
| B | THR303 |
| B | ASP334 |
| B | GLY335 |
| B | GLY336 |
| B | MET355 |
| B | GLY357 |
| B | ASN358 |
| B | TYR381 |
| B | GLY383 |
| B | MET384 |
| B | GLY385 |
| B | GLU412 |
| B | GLY413 |
| B | HOH1006 |
| B | HOH1008 |
| B | HOH1014 |
| B | HOH1030 |
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 | VAL291-THR303 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_01964 |
| Chain | Residue | Details |
| A | CYS301 | |
| B | CYS301 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01964 |
| Chain | Residue | Details |
| A | ARG397 | |
| B | ARG397 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01964 |
| Chain | Residue | Details |
| A | ASP247 | |
| B | HIS468 | |
| A | GLY294 | |
| A | GLU466 | |
| A | SER467 | |
| A | HIS468 | |
| B | ASP247 | |
| B | GLY294 | |
| B | GLU466 | |
| B | SER467 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01964 |
| Chain | Residue | Details |
| A | GLY296 | |
| A | GLY298 | |
| A | CYS301 | |
| B | GLY296 | |
| B | GLY298 | |
| B | CYS301 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER299 | |
| B | GLU412 | |
| A | ASP334 | |
| A | GLY357 | |
| A | TYR381 | |
| A | GLU412 | |
| B | SER299 | |
| B | ASP334 | |
| B | GLY357 | |
| B | TYR381 |
