6I0M
Structure of human IMP dehydrogenase, isoform 2, bound to GDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003938 | molecular_function | IMP dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005778 | cellular_component | peroxisomal membrane |
| 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 | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0097294 | biological_process | 'de novo' XMP biosynthetic process |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003938 | molecular_function | IMP dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005778 | cellular_component | peroxisomal membrane |
| 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 | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0034774 | cellular_component | secretory granule lumen |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0097294 | biological_process | 'de novo' XMP biosynthetic process |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue 5GP A 601 |
| Chain | Residue |
| A | SER68 |
| A | SER388 |
| A | MET414 |
| A | GLY415 |
| A | SO4611 |
| A | HOH717 |
| A | MET70 |
| A | ARG322 |
| A | GLY328 |
| A | THR333 |
| A | ASP364 |
| A | GLY365 |
| A | GLY366 |
| A | GLY387 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue GDP A 602 |
| Chain | Residue |
| A | SER159 |
| A | SER160 |
| A | ARG161 |
| A | ASP162 |
| A | THR180 |
| A | ASP184 |
| A | LEU185 |
| A | VAL186 |
| A | LYS206 |
| A | GLY207 |
| A | LYS208 |
| A | GDP603 |
| B | ARG161 |
| B | LYS205 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue GDP A 603 |
| Chain | Residue |
| A | LYS109 |
| A | TYR110 |
| A | PRO118 |
| A | VAL119 |
| A | PHE139 |
| A | CYS140 |
| A | GLY141 |
| A | LYS208 |
| A | THR225 |
| A | ASP226 |
| A | LYS229 |
| A | GDP602 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GDP A 604 |
| Chain | Residue |
| A | GLU111 |
| A | GLN112 |
| A | ASN198 |
| A | ASP226 |
| A | LEU227 |
| A | ASN230 |
| A | LYS238 |
| A | LYS242 |
| A | HOH710 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | ALA190 |
| A | GLY191 |
| A | ILE192 |
| A | ILE211 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 607 |
| Chain | Residue |
| A | GLY328 |
| A | GLN368 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 608 |
| Chain | Residue |
| A | VAL49 |
| A | ASP50 |
| A | GLN465 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 609 |
| Chain | Residue |
| A | HIS253 |
| A | GLU254 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 610 |
| Chain | Residue |
| A | ALA392 |
| A | THR393 |
| A | ALA396 |
| A | PRO397 |
| A | GLY398 |
| A | TYR400 |
| A | HOH702 |
| B | LEU513 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 611 |
| Chain | Residue |
| A | ASN303 |
| A | GLY324 |
| A | MET325 |
| A | GLY326 |
| A | SER327 |
| A | ASP364 |
| A | 5GP601 |
| A | HOH701 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue 5GP B 601 |
| Chain | Residue |
| B | SER68 |
| B | ARG322 |
| B | GLY328 |
| B | SER329 |
| B | THR333 |
| B | ASP364 |
| B | GLY365 |
| B | GLY366 |
| B | GLY387 |
| B | SER388 |
| B | HOH701 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue GDP B 602 |
| Chain | Residue |
| A | ARG161 |
| A | LYS205 |
| B | SER159 |
| B | SER160 |
| B | ARG161 |
| B | ASP162 |
| B | THR180 |
| B | LEU185 |
| B | LYS206 |
| B | GLY207 |
| B | LYS208 |
| site_id | AD4 |
| Number of Residues | 11 |
| Details | binding site for residue GDP B 603 |
| Chain | Residue |
| B | TYR110 |
| B | PRO118 |
| B | VAL119 |
| B | PHE139 |
| B | CYS140 |
| B | GLY141 |
| B | LYS208 |
| B | THR225 |
| B | ASP226 |
| B | LYS229 |
| B | LYS109 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue GDP B 604 |
| Chain | Residue |
| B | GLU111 |
| B | GLN112 |
| B | GLY113 |
| B | LYS195 |
| B | ASN198 |
| B | ASP226 |
| B | LEU227 |
| B | ASN230 |
| B | LYS238 |
| B | LYS242 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 605 |
| Chain | Residue |
| B | PHE114 |
| B | GLY191 |
| B | ILE192 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 606 |
| Chain | Residue |
| B | VAL49 |
| B | ASP50 |
| B | LEU51 |
| B | LYS62 |
Functional Information from PROSITE/UniProt
| site_id | PS00487 |
| Number of Residues | 13 |
| Details | IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRVGMGsGSICiT |
| Chain | Residue | Details |
| A | LEU321-THR333 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | Domain: {"description":"CBS 2","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| 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"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2002","submissionDatabase":"PDB data bank","title":"Crystal structure of human inosine monophosphate dehydrogenase type II complexed with the MPA/NAD analog C2-MAD.","authors":["Risal D.","Strickler M.D.","Goldstein B.M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
