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4MZ8

Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase, with an Internal Deletion of CBS Domain from Campylobacter jejuni complexed with inhibitor compound C91

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0006164biological_processpurine nucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0006164biological_processpurine nucleotide biosynthetic process
B0016491molecular_functionoxidoreductase activity
C0003824molecular_functioncatalytic activity
C0003938molecular_functionIMP dehydrogenase activity
C0006164biological_processpurine nucleotide biosynthetic process
C0016491molecular_functionoxidoreductase activity
D0003824molecular_functioncatalytic activity
D0003938molecular_functionIMP dehydrogenase activity
D0006164biological_processpurine nucleotide biosynthetic process
D0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE IMP A 501
ChainResidue
AALA46
AGLY336
AMET355
AGLY357
ASER358
ATYR381
AGLY383
AMET384
AGLY385
AGLU411
AGLY412
AMET48
AC91502
AHOH610
AHOH625
AHOH646
AHOH680
AHOH681
AASN273
AGLY298
ASER299
AILE300
ACYS301
AASP334
AGLY335

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE C91 A 502
ChainResidue
AALA246
ATHR303
AMET384
AGLY385
AMET390
ALEU408
AGLU411
AIMP501
BGLY439
BTYR440

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
ATYR378
AARG416
AHOH695
BTHR472

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 504
ChainResidue
ASER422
AARG424
AHOH635

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 505
ChainResidue
AGLN226
AARG229
AHOH668

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 506
ChainResidue
AILE29
AASN40
AASP207
AARG435
AHOH662
AHOH665

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
AARG62
ASER88
AGLU89
ALYS210

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 508
ChainResidue
ATHR460
ATHR460
BTHR460
BTHR460

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 2F2 A 509
ChainResidue
ATYR373
AGLN374
DTYR373
DGLN374

site_idBC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE IMP B 501
ChainResidue
BALA46
BMET48
BASN273
BGLY298
BSER299
BILE300
BCYS301
BASP334
BGLY335
BGLY336
BMET355
BGLY357
BSER358
BTYR381
BGLY383
BMET384
BGLY385
BGLU411
BGLY412
BC91502
BACY506
BHOH615
BHOH623
BHOH627
BHOH685
BHOH689

site_idBC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE C91 B 502
ChainResidue
BACY506
BEDO509
ASER436
AGLY439
ATYR440
BALA246
BTHR303
BGLY385
BMET390
BLEU408
BGLU411
BIMP501

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
ATHR472
BTYR378
BARG416

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 504
ChainResidue
BTYR19

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 B 505
ChainResidue
BARG62

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 506
ChainResidue
BASP244
BSER245
BASN273
BIMP501
BC91502

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 507
ChainResidue
BPHE371
BTYR373
BARG416
CTYR373
CARG416

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 508
ChainResidue
BTYR373
BGLN374
BARG416
CTYR373
CGLN374

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 509
ChainResidue
BSER245
BALA246
BC91502
BHOH620

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT B 510
ChainResidue
BGLN226
BARG229
BHOH672

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 511
ChainResidue
BSER422
BARG424
BHOH622

site_idCC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE IMP C 501
ChainResidue
CALA46
CMET48
CASN273
CGLY298
CSER299
CILE300
CCYS301
CASP334
CGLY335
CGLY336
CMET355
CGLY357
CSER358
CTYR381
CGLY383
CMET384
CGLY385
CGLU411
CGLY412
CC91502
CHOH610
CHOH623
CHOH630
CHOH643

site_idCC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE C91 C 502
ChainResidue
CALA246
CHIS247
CMET390
CGLU411
CIMP501
DPRO24
DGLY439

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 503
ChainResidue
CARG376
CTYR378
CARG416
DTHR472

site_idCC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 504
ChainResidue
CARG80
CARG84

site_idCC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL C 505
ChainResidue
CARG62

site_idCC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 506
ChainResidue
CSER422
CARG424
CHOH642
CHOH646

site_idCC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 507
ChainResidue
CTHR460
CTHR460
DTHR460

site_idDC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE IMP D 501
ChainResidue
DALA46
DMET48
DGLY298
DSER299
DILE300
DCYS301
DASP334
DGLY335
DGLY336
DGLY357
DSER358
DTYR381
DGLY383
DMET384
DGLY385
DGLU411
DGLY412
DC91502
DHOH604

site_idDC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE C91 D 502
ChainResidue
CGLY439
CTYR440
DALA246
DTHR303
DGLY385
DMET390
DGLU411
DIMP501

site_idDC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 503
ChainResidue
CTHR472
DTYR378
DARG416

site_idDC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL D 504
ChainResidue
DSER422
DARG424
DSER425

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT
ChainResidueDetails
AVAL291-THR303

224572

PDB entries from 2024-09-04

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