Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6I0O

Structure of human IMP dehydrogenase, isoform 2, bound to GTP

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
A0046651biological_processlymphocyte proliferation
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0071353biological_processcellular response to interleukin-4
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
B0046651biological_processlymphocyte proliferation
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0071353biological_processcellular response to interleukin-4
B0097294biological_process'de novo' XMP biosynthetic process
B1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue GTP A 601
ChainResidue
AILE157
AGLY207
ALYS208
AGTP602
BARG161
BLYS205
ASER159
ASER160
AASP162
ATHR180
AASP184
ALEU185
AVAL186
ALYS206

site_idAC2
Number of Residues15
Detailsbinding site for residue GTP A 602
ChainResidue
ALYS109
ATYR110
AGLN112
APRO118
AVAL119
ALYS134
APHE139
ACYS140
AGLY141
ASER160
ALYS208
ATHR225
AASP226
ALYS229
AGTP601

site_idAC3
Number of Residues11
Detailsbinding site for residue GTP A 603
ChainResidue
AGLU111
AGLN112
AGLY113
ALEU194
AASN198
AASP226
AASN230
ATYR233
APRO234
ALYS238
ALYS242

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 604
ChainResidue
AVAL49
AASP50
ALEU51
ALYS62
AGLN465

site_idAC5
Number of Residues7
Detailsbinding site for residue SO4 A 605
ChainResidue
ALEU38
APRO39
AGLY40
AMET482
AGLU487
ALEU488
ALYS489

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 A 606
ChainResidue
AILE59
ATHR60
ALYS238

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 A 607
ChainResidue
AGLY191
AILE192
AILE211

site_idAC8
Number of Residues6
Detailsbinding site for residue SO4 A 608
ChainResidue
AGLN202
AARG203
BARG161
BASP162
BPHE165
BLEU166

site_idAC9
Number of Residues3
Detailsbinding site for residue SO4 A 609
ChainResidue
ASER275
AGLN277
AHIS466

site_idAD1
Number of Residues1
Detailsbinding site for residue SO4 A 610
ChainResidue
ASO4611

site_idAD2
Number of Residues5
Detailsbinding site for residue SO4 A 611
ChainResidue
AMET70
AASP364
ASO4610
ASO4612
AHOH707

site_idAD3
Number of Residues5
Detailsbinding site for residue SO4 A 612
ChainResidue
AMET70
AGLY387
ASER388
ASO4611
AHOH706

site_idAD4
Number of Residues3
Detailsbinding site for residue SO4 A 613
ChainResidue
ATYR110
ATYR233
AHIS454

site_idAD5
Number of Residues13
Detailsbinding site for residue GTP B 601
ChainResidue
AARG161
BILE157
BSER159
BSER160
BARG161
BASP162
BASP184
BLEU185
BVAL186
BLYS206
BGLY207
BLYS208
BGTP602

site_idAD6
Number of Residues15
Detailsbinding site for residue GTP B 602
ChainResidue
BGLY138
BPHE139
BCYS140
BGLY141
BSER160
BLYS208
BTHR225
BASP226
BLYS229
BGTP601
BLYS109
BTYR110
BGLN112
BPRO118
BVAL119

site_idAD7
Number of Residues12
Detailsbinding site for residue GTP B 603
ChainResidue
BGLU111
BGLN112
BGLY113
BASN198
BASP226
BLEU227
BASN230
BTYR233
BPRO234
BLYS238
BLYS242
BHOH701

site_idAD8
Number of Residues5
Detailsbinding site for residue SO4 B 604
ChainResidue
BVAL49
BLEU51
BLYS62
BGLN465
BSO4606

site_idAD9
Number of Residues5
Detailsbinding site for residue SO4 B 605
ChainResidue
BLEU38
BPRO39
BGLU487
BLEU488
BLYS489

site_idAE1
Number of Residues3
Detailsbinding site for residue SO4 B 606
ChainResidue
BGLN48
BVAL49
BSO4604

site_idAE2
Number of Residues3
Detailsbinding site for residue SO4 B 607
ChainResidue
BVAL359
BPRO360
BSER382

site_idAE3
Number of Residues2
Detailsbinding site for residue SO4 B 608
ChainResidue
BLYS57
BLYS58

site_idAE4
Number of Residues3
Detailsbinding site for residue SO4 B 609
ChainResidue
BALA264
BVAL268
BASN296

site_idAE5
Number of Residues6
Detailsbinding site for residue SO4 B 610
ChainResidue
BTHR193
BLYS195
BGLU196
BGLU199
BARG355
BHOH704

site_idAE6
Number of Residues1
Detailsbinding site for residue SO4 B 611
ChainResidue
BTYR12

site_idAE7
Number of Residues4
Detailsbinding site for residue SO4 B 612
ChainResidue
BTYR12
BPRO189
BILE192
BARG356

site_idAE8
Number of Residues4
Detailsbinding site for residue SO4 B 613
ChainResidue
BALA190
BGLY191
BILE192
BILE211

site_idAE9
Number of Residues4
Detailsbinding site for residue SO4 B 614
ChainResidue
BLYS58
BTHR60
BLYS238
BLEU245

site_idAF1
Number of Residues6
Detailsbinding site for residue SO4 B 615
ChainResidue
BILE42
BSER275
BSER276
BGLN277
BHIS466
BASP470

site_idAF2
Number of Residues4
Detailsbinding site for residue SO4 B 617
ChainResidue
BLEU84
BTYR110
BTYR233
BHIS454

site_idAF3
Number of Residues1
Detailsbinding site for residue SO4 B 618
ChainResidue
BGLY77

site_idAF4
Number of Residues2
Detailsbinding site for residue SO4 B 619
ChainResidue
BASN312
BHOH705

site_idAF5
Number of Residues4
Detailsbinding site for Ligand GLY B 324 bound to ASN B 303
ChainResidue
BASN303
BVAL323
BMET325
BASP364

site_idAF6
Number of Residues4
Detailsbinding site for Di-peptide LYS B 167 and GLU B 170
ChainResidue
BLEU166
BHIS171
BASP172
BCYS173

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 Residues2
DetailsACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:10097070
ChainResidueDetails
ACYS331
BCYS331

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AARG429
BARG429

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASP274
AASP364
AGLY387
BASP274
BASP364
BGLY387

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AGLY324
BTYR411
BGLN441
BGLU500
BGLY501
BGLY502
ASER329
ATYR411
AGLN441
AGLU500
AGLY501
AGLY502
BGLY324
BSER329

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|Ref.28
ChainResidueDetails
AGLY326
AGLY328
ACYS331
BGLY326
BGLY328
BCYS331

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER122
BSER122

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER160
BSER160

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR400
BTYR400

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER416
BSER416

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS511
BLYS511

site_idSWS_FT_FI11
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS195
ALYS208
ALYS438
BLYS195
BLYS208
BLYS438

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon