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4Z87

Structure of the IMP dehydrogenase from Ashbya gossypii bound to GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006183biological_processGTP biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0003938molecular_functionIMP dehydrogenase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006164biological_processpurine nucleotide biosynthetic process
C0006177biological_processGMP biosynthetic process
C0006183biological_processGTP biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0003938molecular_functionIMP dehydrogenase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006164biological_processpurine nucleotide biosynthetic process
D0006177biological_processGMP biosynthetic process
D0006183biological_processGTP biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue 5GP A 601
ChainResidue
ASER74
AGLY368
AGLY369
AMET388
AGLY390
AGLY391
ATYR414
AGLY416
AMET417
AGLY418
ASER419
AMET76
AGLN448
AGLY449
AHOH708
AHOH785
AARG325
AGLY331
ASER332
AILE333
ACYS334
ATHR336
AASP367

site_idAC2
Number of Residues17
Detailsbinding site for residue GDP A 602
ChainResidue
ATHR165
ASER166
AASP168
ATHR184
AASP186
AVAL187
AILE188
ALYS208
AGLY209
AHOH703
AHOH705
AHOH754
AHOH782
AHOH790
AHOH812
BARG167
BLYS207

site_idAC3
Number of Residues16
Detailsbinding site for residue GDP A 603
ChainResidue
ALYS115
ATYR116
AASN118
APRO124
AVAL125
APHE145
AALA146
AGLY147
ALYS210
ASER225
ATHR227
AASP228
ALYS231
AHOH742
AHOH773
AHOH775

site_idAC4
Number of Residues14
Detailsbinding site for residue GDP A 604
ChainResidue
AGLU117
AASN118
AGLY119
ALEU196
AGLU197
AASN200
AASP228
ALEU229
AASN232
ALYS240
ALYS245
AHOH701
DTHR8
DGLU11

site_idAC5
Number of Residues6
Detailsbinding site for residue K A 605
ChainResidue
AGLY329
AGLY331
ACYS334
AGLU507
AGLY508
AGLY509

site_idAC6
Number of Residues4
Detailsbinding site for residue ACT A 606
ChainResidue
ASER58
ATHR66
AASN68
DASP5

site_idAC7
Number of Residues20
Detailsbinding site for residue 5GP B 601
ChainResidue
BHOH790
BSER74
BMET76
BASN306
BARG325
BGLY331
BSER332
BCYS334
BTHR336
BASP367
BGLY369
BMET388
BGLY390
BGLY391
BTYR414
BGLY416
BMET417
BGLY418
BGLN448
BHOH736

site_idAC8
Number of Residues16
Detailsbinding site for residue GDP B 602
ChainResidue
AARG167
ALYS207
BTHR165
BSER166
BARG167
BASP168
BTHR184
BASP186
BVAL187
BILE188
BLYS208
BGLY209
BHOH734
BHOH743
BHOH764
BHOH783

site_idAC9
Number of Residues16
Detailsbinding site for residue GDP B 603
ChainResidue
BLYS115
BTYR116
BASN118
BPRO124
BVAL125
BPHE145
BALA146
BGLY147
BLYS210
BSER225
BTHR227
BASP228
BLYS231
BHOH709
BHOH711
BHOH727

site_idAD1
Number of Residues10
Detailsbinding site for residue GDP B 604
ChainResidue
BGLU117
BASN118
BGLY119
BASN200
BASP228
BLEU229
BASN232
BPRO236
BLYS240
BLYS245

site_idAD2
Number of Residues6
Detailsbinding site for residue K B 605
ChainResidue
BGLY329
BGLY331
BCYS334
BGLU507
BGLY508
BGLY509

site_idAD3
Number of Residues2
Detailsbinding site for residue ACT B 606
ChainResidue
BLEU91
BILE464

site_idAD4
Number of Residues23
Detailsbinding site for residue 5GP C 601
ChainResidue
CSER74
CMET76
CASN306
CARG325
CGLY331
CSER332
CILE333
CCYS334
CTHR336
CASP367
CGLY369
CMET388
CGLY390
CGLY391
CTYR414
CGLY416
CMET417
CGLY418
CGLN448
CGLY449
CACT606
CHOH738
CHOH746

site_idAD5
Number of Residues11
Detailsbinding site for residue GDP C 602
ChainResidue
CTHR165
CSER166
CASP168
CTHR184
CASP186
CVAL187
CILE188
CLYS208
CGLY209
DARG167
DLYS207

site_idAD6
Number of Residues15
Detailsbinding site for residue GDP C 603
ChainResidue
CLYS115
CTYR116
CASN118
CILE121
CPRO124
CVAL125
CPHE145
CALA146
CGLY147
CLYS210
CSER225
CTHR227
CASP228
CLYS231
CHOH712

site_idAD7
Number of Residues13
Detailsbinding site for residue GDP C 604
ChainResidue
BALA7
BGLU11
BHIS318
CGLU117
CASN118
CGLY119
CLEU196
CASN200
CASP228
CLEU229
CASN232
CLYS240
CLYS245

site_idAD8
Number of Residues6
Detailsbinding site for residue K C 605
ChainResidue
CGLY329
CGLY331
CCYS334
CGLU507
CGLY508
CGLY509

site_idAD9
Number of Residues4
Detailsbinding site for residue ACT C 606
ChainResidue
CASP277
CSER278
CARG325
C5GP601

site_idAE1
Number of Residues2
Detailsbinding site for residue ACT C 607
ChainResidue
CLEU91
CTYR468

site_idAE2
Number of Residues21
Detailsbinding site for residue 5GP D 600
ChainResidue
DSER74
DMET76
DARG325
DGLY331
DSER332
DILE333
DCYS334
DTHR336
DASP367
DGLY369
DMET388
DGLY390
DGLY391
DTYR414
DGLY416
DMET417
DGLY418
DGLN448
DGLY449
DHOH712
DHOH739

site_idAE3
Number of Residues14
Detailsbinding site for residue GDP D 601
ChainResidue
CARG167
CLYS207
DTHR165
DSER166
DARG167
DASP168
DTHR184
DASP186
DVAL187
DILE188
DLYS208
DGLY209
DHOH701
DHOH758

site_idAE4
Number of Residues14
Detailsbinding site for residue GDP D 602
ChainResidue
DLYS115
DTYR116
DASN118
DPRO124
DVAL125
DPHE145
DALA146
DGLY147
DLYS210
DSER225
DTHR227
DASP228
DLYS231
DHOH758

site_idAE5
Number of Residues9
Detailsbinding site for residue GDP D 603
ChainResidue
DGLU117
DASN118
DGLY119
DASN200
DASP228
DASN232
DLYS240
DLYS245
DHOH711

site_idAE6
Number of Residues6
Detailsbinding site for residue K D 604
ChainResidue
DGLY329
DGLY331
DCYS334
DGLU507
DGLY508
DGLY509

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRIGMGsGSICiT
ChainResidueDetails
ALEU324-THR336

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PDB entries from 2024-07-24

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