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6UAJ

Human IMPDH2 treated with ATP, IMP, NAD+, and 2 mM GTP. Free canonical octamer reconstruction.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003677molecular_functionDNA binding
A0003723molecular_functionRNA binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005778cellular_componentperoxisomal membrane
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0007623biological_processcircadian rhythm
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0034774cellular_componentsecretory granule lumen
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0097294biological_process'de novo' XMP biosynthetic process
A1904813cellular_componentficolin-1-rich granule lumen
B0000166molecular_functionnucleotide binding
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005778cellular_componentperoxisomal membrane
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006183biological_processGTP biosynthetic process
B0007623biological_processcircadian rhythm
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0034774cellular_componentsecretory granule lumen
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0097294biological_process'de novo' XMP biosynthetic process
B1904813cellular_componentficolin-1-rich granule lumen
C0000166molecular_functionnucleotide binding
C0003677molecular_functionDNA binding
C0003723molecular_functionRNA binding
C0003824molecular_functioncatalytic activity
C0003938molecular_functionIMP dehydrogenase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005778cellular_componentperoxisomal membrane
C0005829cellular_componentcytosol
C0006164biological_processpurine nucleotide biosynthetic process
C0006177biological_processGMP biosynthetic process
C0006183biological_processGTP biosynthetic process
C0007623biological_processcircadian rhythm
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0034774cellular_componentsecretory granule lumen
C0046872molecular_functionmetal ion binding
C0070062cellular_componentextracellular exosome
C0097294biological_process'de novo' XMP biosynthetic process
C1904813cellular_componentficolin-1-rich granule lumen
D0000166molecular_functionnucleotide binding
D0003677molecular_functionDNA binding
D0003723molecular_functionRNA binding
D0003824molecular_functioncatalytic activity
D0003938molecular_functionIMP dehydrogenase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005778cellular_componentperoxisomal membrane
D0005829cellular_componentcytosol
D0006164biological_processpurine nucleotide biosynthetic process
D0006177biological_processGMP biosynthetic process
D0006183biological_processGTP biosynthetic process
D0007623biological_processcircadian rhythm
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0034774cellular_componentsecretory granule lumen
D0046872molecular_functionmetal ion binding
D0070062cellular_componentextracellular exosome
D0097294biological_process'de novo' XMP biosynthetic process
D1904813cellular_componentficolin-1-rich granule lumen
E0000166molecular_functionnucleotide binding
E0003677molecular_functionDNA binding
E0003723molecular_functionRNA binding
E0003824molecular_functioncatalytic activity
E0003938molecular_functionIMP dehydrogenase activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005778cellular_componentperoxisomal membrane
E0005829cellular_componentcytosol
E0006164biological_processpurine nucleotide biosynthetic process
E0006177biological_processGMP biosynthetic process
E0006183biological_processGTP biosynthetic process
E0007623biological_processcircadian rhythm
E0016020cellular_componentmembrane
E0016491molecular_functionoxidoreductase activity
E0034774cellular_componentsecretory granule lumen
E0046872molecular_functionmetal ion binding
E0070062cellular_componentextracellular exosome
E0097294biological_process'de novo' XMP biosynthetic process
E1904813cellular_componentficolin-1-rich granule lumen
F0000166molecular_functionnucleotide binding
F0003677molecular_functionDNA binding
F0003723molecular_functionRNA binding
F0003824molecular_functioncatalytic activity
F0003938molecular_functionIMP dehydrogenase activity
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005778cellular_componentperoxisomal membrane
F0005829cellular_componentcytosol
F0006164biological_processpurine nucleotide biosynthetic process
F0006177biological_processGMP biosynthetic process
F0006183biological_processGTP biosynthetic process
F0007623biological_processcircadian rhythm
F0016020cellular_componentmembrane
F0016491molecular_functionoxidoreductase activity
F0034774cellular_componentsecretory granule lumen
F0046872molecular_functionmetal ion binding
F0070062cellular_componentextracellular exosome
F0097294biological_process'de novo' XMP biosynthetic process
F1904813cellular_componentficolin-1-rich granule lumen
G0000166molecular_functionnucleotide binding
G0003677molecular_functionDNA binding
G0003723molecular_functionRNA binding
G0003824molecular_functioncatalytic activity
G0003938molecular_functionIMP dehydrogenase activity
G0005515molecular_functionprotein binding
G0005576cellular_componentextracellular region
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005778cellular_componentperoxisomal membrane
G0005829cellular_componentcytosol
G0006164biological_processpurine nucleotide biosynthetic process
G0006177biological_processGMP biosynthetic process
G0006183biological_processGTP biosynthetic process
G0007623biological_processcircadian rhythm
G0016020cellular_componentmembrane
G0016491molecular_functionoxidoreductase activity
G0034774cellular_componentsecretory granule lumen
G0046872molecular_functionmetal ion binding
G0070062cellular_componentextracellular exosome
G0097294biological_process'de novo' XMP biosynthetic process
G1904813cellular_componentficolin-1-rich granule lumen
H0000166molecular_functionnucleotide binding
H0003677molecular_functionDNA binding
H0003723molecular_functionRNA binding
H0003824molecular_functioncatalytic activity
H0003938molecular_functionIMP dehydrogenase activity
H0005515molecular_functionprotein binding
H0005576cellular_componentextracellular region
H0005634cellular_componentnucleus
H0005737cellular_componentcytoplasm
H0005778cellular_componentperoxisomal membrane
H0005829cellular_componentcytosol
H0006164biological_processpurine nucleotide biosynthetic process
H0006177biological_processGMP biosynthetic process
H0006183biological_processGTP biosynthetic process
H0007623biological_processcircadian rhythm
H0016020cellular_componentmembrane
H0016491molecular_functionoxidoreductase activity
H0034774cellular_componentsecretory granule lumen
H0046872molecular_functionmetal ion binding
H0070062cellular_componentextracellular exosome
H0097294biological_process'de novo' XMP biosynthetic process
H1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue GTP A 601
ChainResidue
ATYR110
AATP603
AGLN112
AILE115
APRO118
APHE139
ACYS140
AGLY141
ASER160
ATHR225

site_idAC2
Number of Residues9
Detailsbinding site for residue GTP A 602
ChainResidue
ALEU194
ALYS195
AASN198
AASP226
ALEU227
AASN230
APRO234
ALYS238
ALYS242

site_idAC3
Number of Residues12
Detailsbinding site for residue ATP A 603
ChainResidue
ASER159
ASER160
AARG161
ATHR180
AASP184
ALEU185
AVAL186
ALYS206
AGLY207
ALYS208
AGTP601
FARG224

site_idAC4
Number of Residues15
Detailsbinding site for residue IMP A 604
ChainResidue
ASER68
AMET70
AARG322
AILE330
ACYS331
AASP364
AGLY365
AILE367
AGLY387
ASER388
ATYR411
AGLY413
AMET414
AGLY415
ANAD605

site_idAC5
Number of Residues13
Detailsbinding site for residue NAD A 605
ChainResidue
ATHR252
AHIS253
AASP274
ASER275
ASER276
APHE282
AASN303
AASP364
AMET414
AGLN441
AIMP604
DILE42
DGLN469

site_idAC6
Number of Residues10
Detailsbinding site for residue GTP B 601
ChainResidue
BTYR110
BGLN112
BILE115
BPRO118
BPHE139
BCYS140
BGLY141
BSER160
BTHR225
BATP603

site_idAC7
Number of Residues15
Detailsbinding site for residue IMP B 604
ChainResidue
BSER68
BMET70
BARG322
BILE330
BCYS331
BASP364
BGLY365
BILE367
BGLY387
BSER388
BTYR411
BGLY413
BMET414
BGLY415
BNAD605

site_idAC8
Number of Residues13
Detailsbinding site for residue NAD B 605
ChainResidue
AILE42
AGLN469
BTHR252
BHIS253
BASP274
BSER275
BSER276
BPHE282
BASN303
BASP364
BMET414
BGLN441
BIMP604

site_idAC9
Number of Residues10
Detailsbinding site for residue GTP C 601
ChainResidue
CILE115
CPRO118
CPHE139
CCYS140
CGLY141
CSER160
CTHR225
CATP603
CTYR110
CGLN112

site_idAD1
Number of Residues15
Detailsbinding site for residue IMP C 604
ChainResidue
CSER68
CMET70
CARG322
CILE330
CCYS331
CASP364
CGLY365
CILE367
CGLY387
CSER388
CTYR411
CGLY413
CMET414
CGLY415
CNAD605

site_idAD2
Number of Residues13
Detailsbinding site for residue NAD C 605
ChainResidue
BILE42
BGLN469
CTHR252
CHIS253
CASP274
CSER275
CSER276
CPHE282
CASN303
CASP364
CMET414
CGLN441
CIMP604

site_idAD3
Number of Residues10
Detailsbinding site for residue GTP D 601
ChainResidue
DTYR110
DGLN112
DILE115
DPRO118
DPHE139
DCYS140
DGLY141
DSER160
DTHR225
DATP603

site_idAD4
Number of Residues15
Detailsbinding site for residue IMP D 604
ChainResidue
DSER68
DMET70
DARG322
DILE330
DCYS331
DASP364
DGLY365
DILE367
DGLY387
DSER388
DTYR411
DGLY413
DMET414
DGLY415
DNAD605

site_idAD5
Number of Residues13
Detailsbinding site for residue NAD D 605
ChainResidue
CILE42
CGLN469
DTHR252
DHIS253
DASP274
DSER275
DSER276
DPHE282
DASN303
DASP364
DMET414
DGLN441
DIMP604

site_idAD6
Number of Residues10
Detailsbinding site for residue GTP E 601
ChainResidue
ETYR110
EGLN112
EILE115
EPRO118
EPHE139
ECYS140
EGLY141
ESER160
ETHR225
EATP603

site_idAD7
Number of Residues15
Detailsbinding site for residue IMP E 604
ChainResidue
ESER68
EMET70
EARG322
EILE330
ECYS331
EASP364
EGLY365
EILE367
EGLY387
ESER388
ETYR411
EGLY413
EMET414
EGLY415
ENAD605

site_idAD8
Number of Residues13
Detailsbinding site for residue NAD E 605
ChainResidue
ETHR252
EHIS253
EASP274
ESER275
ESER276
EPHE282
EASN303
EASP364
EMET414
EGLN441
EIMP604
HILE42
HGLN469

site_idAD9
Number of Residues10
Detailsbinding site for residue GTP F 601
ChainResidue
FTYR110
FGLN112
FILE115
FPRO118
FPHE139
FCYS140
FGLY141
FSER160
FTHR225
FATP603

site_idAE1
Number of Residues15
Detailsbinding site for residue IMP F 604
ChainResidue
FSER68
FMET70
FARG322
FILE330
FCYS331
FASP364
FGLY365
FILE367
FGLY387
FSER388
FTYR411
FGLY413
FMET414
FGLY415
FNAD605

site_idAE2
Number of Residues13
Detailsbinding site for residue NAD F 605
ChainResidue
EILE42
EGLN469
FTHR252
FHIS253
FASP274
FSER275
FSER276
FPHE282
FASN303
FASP364
FMET414
FGLN441
FIMP604

site_idAE3
Number of Residues10
Detailsbinding site for residue GTP G 601
ChainResidue
GTYR110
GGLN112
GILE115
GPRO118
GPHE139
GCYS140
GGLY141
GSER160
GTHR225
GATP603

site_idAE4
Number of Residues15
Detailsbinding site for residue IMP G 604
ChainResidue
GSER68
GMET70
GARG322
GILE330
GCYS331
GASP364
GGLY365
GILE367
GGLY387
GSER388
GTYR411
GGLY413
GMET414
GGLY415
GNAD605

site_idAE5
Number of Residues13
Detailsbinding site for residue NAD G 605
ChainResidue
FILE42
FGLN469
GTHR252
GHIS253
GASP274
GSER275
GSER276
GPHE282
GASN303
GASP364
GMET414
GGLN441
GIMP604

site_idAE6
Number of Residues10
Detailsbinding site for residue GTP H 601
ChainResidue
HTYR110
HGLN112
HILE115
HPRO118
HPHE139
HCYS140
HGLY141
HSER160
HTHR225
HATP603

site_idAE7
Number of Residues15
Detailsbinding site for residue IMP H 604
ChainResidue
HSER68
HMET70
HARG322
HILE330
HCYS331
HASP364
HGLY365
HILE367
HGLY387
HSER388
HTYR411
HGLY413
HMET414
HGLY415
HNAD605

site_idAE8
Number of Residues13
Detailsbinding site for residue NAD H 605
ChainResidue
GILE42
GGLN469
HTHR252
HHIS253
HASP274
HSER275
HSER276
HPHE282
HASN303
HASP364
HMET414
HGLN441
HIMP604

site_idAE9
Number of Residues13
Detailsbinding site for Di-peptide GTP B 602 and ASP B 226
ChainResidue
BGLN112
BLEU194
BLYS195
BASN198
BARG224
BTHR225
BLEU227
BLYS228
BLYS229
BASN230
BPRO234
BLYS238
BLYS242

site_idAF1
Number of Residues15
Detailsbinding site for Di-peptide ATP B 603 and ARG B 161
ChainResidue
BSER159
BSER160
BASP162
BILE163
BASP164
BPHE165
BTHR180
BASP184
BLEU185
BVAL186
BLYS206
BGLY207
BLYS208
BGTP601
EARG224

site_idAF2
Number of Residues13
Detailsbinding site for Di-peptide GTP C 602 and ASP C 226
ChainResidue
CGLN112
CLEU194
CLYS195
CASN198
CARG224
CTHR225
CLEU227
CLYS228
CLYS229
CASN230
CPRO234
CLYS238
CLYS242

site_idAF3
Number of Residues15
Detailsbinding site for Di-peptide ATP C 603 and ARG C 161
ChainResidue
CSER159
CSER160
CASP162
CILE163
CASP164
CPHE165
CTHR180
CASP184
CLEU185
CVAL186
CLYS206
CGLY207
CLYS208
CGTP601
HARG224

site_idAF4
Number of Residues13
Detailsbinding site for Di-peptide GTP D 602 and ASP D 226
ChainResidue
DGLN112
DLEU194
DLYS195
DASN198
DARG224
DTHR225
DLEU227
DLYS228
DLYS229
DASN230
DPRO234
DLYS238
DLYS242

site_idAF5
Number of Residues15
Detailsbinding site for Di-peptide ATP D 603 and ARG D 161
ChainResidue
DSER159
DSER160
DASP162
DILE163
DASP164
DPHE165
DTHR180
DASP184
DLEU185
DVAL186
DLYS206
DGLY207
DLYS208
DGTP601
GARG224

site_idAF6
Number of Residues13
Detailsbinding site for Di-peptide GTP E 602 and ASP E 226
ChainResidue
EGLN112
ELEU194
ELYS195
EASN198
EARG224
ETHR225
ELEU227
ELYS228
ELYS229
EASN230
EPRO234
ELYS238
ELYS242

site_idAF7
Number of Residues15
Detailsbinding site for Di-peptide ATP E 603 and ARG E 161
ChainResidue
BARG224
ESER159
ESER160
EASP162
EILE163
EASP164
EPHE165
ETHR180
EASP184
ELEU185
EVAL186
ELYS206
EGLY207
ELYS208
EGTP601

site_idAF8
Number of Residues13
Detailsbinding site for Di-peptide GTP F 602 and ASP F 226
ChainResidue
FGLN112
FLEU194
FLYS195
FASN198
FARG224
FTHR225
FLEU227
FLYS228
FLYS229
FASN230
FPRO234
FLYS238
FLYS242

site_idAF9
Number of Residues15
Detailsbinding site for Di-peptide ATP F 603 and ARG F 161
ChainResidue
AARG224
FSER159
FSER160
FASP162
FILE163
FASP164
FPHE165
FTHR180
FASP184
FLEU185
FVAL186
FLYS206
FGLY207
FLYS208
FGTP601

site_idAG1
Number of Residues13
Detailsbinding site for Di-peptide GTP G 602 and ASP G 226
ChainResidue
GGLN112
GLEU194
GLYS195
GASN198
GARG224
GTHR225
GLEU227
GLYS228
GLYS229
GASN230
GPRO234
GLYS238
GLYS242

site_idAG2
Number of Residues15
Detailsbinding site for Di-peptide ATP G 603 and ARG G 161
ChainResidue
DARG224
GSER159
GSER160
GASP162
GILE163
GASP164
GPHE165
GTHR180
GASP184
GLEU185
GVAL186
GLYS206
GGLY207
GLYS208
GGTP601

site_idAG3
Number of Residues13
Detailsbinding site for Di-peptide GTP H 602 and ASP H 226
ChainResidue
HGLN112
HLEU194
HLYS195
HASN198
HARG224
HTHR225
HLEU227
HLYS228
HLYS229
HASN230
HPRO234
HLYS238
HLYS242

site_idAG4
Number of Residues15
Detailsbinding site for Di-peptide ATP H 603 and ARG H 161
ChainResidue
CARG224
HSER159
HSER160
HASP162
HILE163
HASP164
HPHE165
HTHR180
HASP184
HLEU185
HVAL186
HLYS206
HGLY207
HLYS208
HGTP601

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRVGMGsGSICiT
ChainResidueDetails
ALEU321-THR333

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues472
DetailsDomain: {"description":"CBS 1","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues464
DetailsDomain: {"description":"CBS 2","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsActive site: {"description":"Thioimidate intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10097070","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues40
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues88
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues24
DetailsBinding 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."]}}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsModified 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"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues8
DetailsModified 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"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues32
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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