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 | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006177 | biological_process | GMP biosynthetic process |
| A | 0006183 | biological_process | GTP biosynthetic process |
| A | 0007623 | biological_process | circadian rhythm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046651 | biological_process | lymphocyte proliferation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071353 | biological_process | cellular response to interleukin-4 |
| A | 0097294 | biological_process | 'de novo' XMP biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003938 | molecular_function | IMP dehydrogenase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006177 | biological_process | GMP biosynthetic process |
| B | 0006183 | biological_process | GTP biosynthetic process |
| B | 0007623 | biological_process | circadian rhythm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046651 | biological_process | lymphocyte proliferation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071353 | biological_process | cellular response to interleukin-4 |
| B | 0097294 | biological_process | 'de novo' XMP biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K A 601 |
| Chain | Residue |
| A | GLY326 |
| A | CYS327 |
| A | GLY328 |
| A | CYS331 |
| A | GLU500 |
| A | GLY501 |
| A | GLY502 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 602 |
| Chain | Residue |
| B | CYS331 |
| B | GLU500 |
| B | GLY501 |
| B | GLY502 |
| B | GLY326 |
| B | GLY328 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE IMP A 1331 |
| Chain | Residue |
| A | SER68 |
| A | MET70 |
| A | ARG322 |
| A | GLY328 |
| A | SER329 |
| A | CYS331 |
| A | ASP364 |
| A | GLY366 |
| A | MET386 |
| A | GLY387 |
| A | SER388 |
| A | TYR411 |
| A | GLY413 |
| A | MET414 |
| A | GLY415 |
| A | GLN441 |
| A | GLY442 |
| A | HOH617 |
| A | HOH653 |
| A | HOH664 |
| A | HOH738 |
| A | MOA1332 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE IMP B 1332 |
| Chain | Residue |
| B | SER68 |
| B | MET70 |
| B | ARG322 |
| B | GLY328 |
| B | SER329 |
| B | CYS331 |
| B | ASP364 |
| B | GLY366 |
| B | MET385 |
| B | GLY387 |
| B | SER388 |
| B | TYR411 |
| B | GLY413 |
| B | MET414 |
| B | GLY415 |
| B | GLN441 |
| B | GLY442 |
| B | HOH708 |
| B | HOH710 |
| B | HOH714 |
| B | HOH794 |
| B | MOA1333 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE MOA A 1332 |
| Chain | Residue |
| A | ASP274 |
| A | SER275 |
| A | SER276 |
| A | ASN303 |
| A | GLY324 |
| A | MET325 |
| A | GLY326 |
| A | CYS331 |
| A | THR333 |
| A | MET414 |
| A | GLY415 |
| A | GLN441 |
| A | HOH658 |
| A | HOH773 |
| A | IMP1331 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MOA B 1333 |
| Chain | Residue |
| B | ASP274 |
| B | SER275 |
| B | SER276 |
| B | ASN303 |
| B | GLY324 |
| B | MET325 |
| B | GLY326 |
| B | THR333 |
| B | GLY415 |
| B | GLN441 |
| B | HOH725 |
| B | HOH770 |
| B | IMP1332 |
Functional Information from PROSITE/UniProt
| site_id | PS00487 |
| Number of Residues | 13 |
| Details | IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRVGMGcGSICiT |
| Chain | Residue | Details |
| A | LEU321-THR333 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Thioimidate intermediate"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8681386","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JR1","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P12268","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P12268","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P12268","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 5 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P12268","evidenceCode":"ECO:0000250"}]} |
