6I0O
Structure of human IMP dehydrogenase, isoform 2, bound to GTP
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 GTP A 601 |
| Chain | Residue |
| A | ILE157 |
| A | GLY207 |
| A | LYS208 |
| A | GTP602 |
| B | ARG161 |
| B | LYS205 |
| A | SER159 |
| A | SER160 |
| A | ASP162 |
| A | THR180 |
| A | ASP184 |
| A | LEU185 |
| A | VAL186 |
| A | LYS206 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue GTP A 602 |
| Chain | Residue |
| A | LYS109 |
| A | TYR110 |
| A | GLN112 |
| A | PRO118 |
| A | VAL119 |
| A | LYS134 |
| A | PHE139 |
| A | CYS140 |
| A | GLY141 |
| A | SER160 |
| A | LYS208 |
| A | THR225 |
| A | ASP226 |
| A | LYS229 |
| A | GTP601 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue GTP A 603 |
| Chain | Residue |
| A | GLU111 |
| A | GLN112 |
| A | GLY113 |
| A | LEU194 |
| A | ASN198 |
| A | ASP226 |
| A | ASN230 |
| A | TYR233 |
| A | PRO234 |
| A | LYS238 |
| A | LYS242 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | VAL49 |
| A | ASP50 |
| A | LEU51 |
| A | LYS62 |
| A | GLN465 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | LEU38 |
| A | PRO39 |
| A | GLY40 |
| A | MET482 |
| A | GLU487 |
| A | LEU488 |
| A | LYS489 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | ILE59 |
| A | THR60 |
| A | LYS238 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 607 |
| Chain | Residue |
| A | GLY191 |
| A | ILE192 |
| A | ILE211 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 608 |
| Chain | Residue |
| A | GLN202 |
| A | ARG203 |
| B | ARG161 |
| B | ASP162 |
| B | PHE165 |
| B | LEU166 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 609 |
| Chain | Residue |
| A | SER275 |
| A | GLN277 |
| A | HIS466 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 610 |
| Chain | Residue |
| A | SO4611 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 611 |
| Chain | Residue |
| A | MET70 |
| A | ASP364 |
| A | SO4610 |
| A | SO4612 |
| A | HOH707 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 612 |
| Chain | Residue |
| A | MET70 |
| A | GLY387 |
| A | SER388 |
| A | SO4611 |
| A | HOH706 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 613 |
| Chain | Residue |
| A | TYR110 |
| A | TYR233 |
| A | HIS454 |
| site_id | AD5 |
| Number of Residues | 13 |
| Details | binding site for residue GTP B 601 |
| Chain | Residue |
| A | ARG161 |
| B | ILE157 |
| B | SER159 |
| B | SER160 |
| B | ARG161 |
| B | ASP162 |
| B | ASP184 |
| B | LEU185 |
| B | VAL186 |
| B | LYS206 |
| B | GLY207 |
| B | LYS208 |
| B | GTP602 |
| site_id | AD6 |
| Number of Residues | 15 |
| Details | binding site for residue GTP B 602 |
| Chain | Residue |
| B | GLY138 |
| B | PHE139 |
| B | CYS140 |
| B | GLY141 |
| B | SER160 |
| B | LYS208 |
| B | THR225 |
| B | ASP226 |
| B | LYS229 |
| B | GTP601 |
| B | LYS109 |
| B | TYR110 |
| B | GLN112 |
| B | PRO118 |
| B | VAL119 |
| site_id | AD7 |
| Number of Residues | 12 |
| Details | binding site for residue GTP B 603 |
| Chain | Residue |
| B | GLU111 |
| B | GLN112 |
| B | GLY113 |
| B | ASN198 |
| B | ASP226 |
| B | LEU227 |
| B | ASN230 |
| B | TYR233 |
| B | PRO234 |
| B | LYS238 |
| B | LYS242 |
| B | HOH701 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 604 |
| Chain | Residue |
| B | VAL49 |
| B | LEU51 |
| B | LYS62 |
| B | GLN465 |
| B | SO4606 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 605 |
| Chain | Residue |
| B | LEU38 |
| B | PRO39 |
| B | GLU487 |
| B | LEU488 |
| B | LYS489 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 606 |
| Chain | Residue |
| B | GLN48 |
| B | VAL49 |
| B | SO4604 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 607 |
| Chain | Residue |
| B | VAL359 |
| B | PRO360 |
| B | SER382 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 608 |
| Chain | Residue |
| B | LYS57 |
| B | LYS58 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 609 |
| Chain | Residue |
| B | ALA264 |
| B | VAL268 |
| B | ASN296 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 610 |
| Chain | Residue |
| B | THR193 |
| B | LYS195 |
| B | GLU196 |
| B | GLU199 |
| B | ARG355 |
| B | HOH704 |
| site_id | AE6 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 611 |
| Chain | Residue |
| B | TYR12 |
| site_id | AE7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 612 |
| Chain | Residue |
| B | TYR12 |
| B | PRO189 |
| B | ILE192 |
| B | ARG356 |
| site_id | AE8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 613 |
| Chain | Residue |
| B | ALA190 |
| B | GLY191 |
| B | ILE192 |
| B | ILE211 |
| site_id | AE9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 614 |
| Chain | Residue |
| B | LYS58 |
| B | THR60 |
| B | LYS238 |
| B | LEU245 |
| site_id | AF1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 615 |
| Chain | Residue |
| B | ILE42 |
| B | SER275 |
| B | SER276 |
| B | GLN277 |
| B | HIS466 |
| B | ASP470 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 617 |
| Chain | Residue |
| B | LEU84 |
| B | TYR110 |
| B | TYR233 |
| B | HIS454 |
| site_id | AF3 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 618 |
| Chain | Residue |
| B | GLY77 |
| site_id | AF4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 619 |
| Chain | Residue |
| B | ASN312 |
| B | HOH705 |
| site_id | AF5 |
| Number of Residues | 4 |
| Details | binding site for Ligand GLY B 324 bound to ASN B 303 |
| Chain | Residue |
| B | ASN303 |
| B | VAL323 |
| B | MET325 |
| B | ASP364 |
| site_id | AF6 |
| Number of Residues | 4 |
| Details | binding site for Di-peptide LYS B 167 and GLU B 170 |
| Chain | Residue |
| B | LEU166 |
| B | HIS171 |
| B | ASP172 |
| B | CYS173 |
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 | 59 |
| Details | Domain: {"description":"CBS 1","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 116 |
| Details | Domain: {"description":"CBS 2","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| 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_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| 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 |
