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4MZ1

Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase, with a Internal Deletion of CBS Domain from Campylobacter jejuni complexed with inhibitor compound P12

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
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE IMP A 500
ChainResidue
AALA46
AMET355
AGLY357
ASER358
ATYR381
AGLY383
AMET384
AGLY385
AGLU411
AGLY412
A2F1501
AMET48
AHOH601
AHOH606
AHOH610
AHOH615
AHOH628
AGLY298
ASER299
AILE300
ACYS301
AASP334
AGLY335
AGLY336

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 2F1 A 501
ChainResidue
AVAL22
AALA246
ATHR303
AGLY385
AGLU411
AGLY439
ATYR440
AIMP500

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 502
ChainResidue
AGLY296
AGLY298
ACYS301
AGLU465
ASER466
AHIS467

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AHIS54
AARG55

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PO4 A 504
ChainResidue
AARG62

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 505
ChainResidue
ATYR378
AARG416
ATHR472

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 506
ChainResidue
ATYR373
ATYR373
AGLN374
AGLN374

site_idAC8
Number of Residues24
DetailsBINDING SITE FOR RESIDUE IMP B 500
ChainResidue
BALA46
BMET48
BASN273
BGLY298
BSER299
BILE300
BCYS301
BASP334
BGLY335
BGLY336
BMET355
BGLY357
BSER358
BTYR381
BGLY383
BMET384
BGLY385
BGLU411
BGLY412
B2F1501
BHOH604
BHOH636
BHOH637
BHOH654

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 2F1 B 501
ChainResidue
BALA246
BTHR303
BMET384
BGLY385
BMET390
BGLU411
BGLY439
BTYR440
BIMP500

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 502
ChainResidue
BGLY296
BGLY298
BCYS301
BGLU465
BSER466
BHIS467

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 503
ChainResidue
BTYR378
BARG416
BTHR472

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 B 504
ChainResidue
BARG62

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 B 505
ChainResidue
BHIS54

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 506
ChainResidue
BGLN226
BARG229

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY C 501
ChainResidue
BTYR373
BGLN374
CTYR373

site_idBC7
Number of Residues23
DetailsBINDING SITE FOR RESIDUE IMP C 502
ChainResidue
CGLY298
CSER299
CILE300
CCYS301
CASP334
CGLY335
CGLY336
CMET355
CGLY357
CSER358
CTYR381
CGLY383
CMET384
CGLY385
CGLU411
CGLY412
C2F1503
CHOH615
CHOH625
CHOH655
CHOH656
CALA46
CMET48

site_idBC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 2F1 C 503
ChainResidue
CALA246
CHIS247
CTHR303
CMET384
CGLY385
CMET390
CGLU411
CGLY439
CTYR440
CIMP502

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K C 504
ChainResidue
CGLY296
CGLY298
CCYS301
CGLU465
CSER466
CHIS467

site_idCC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 C 505
ChainResidue
CHIS54

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 C 506
ChainResidue
CARG376
CTYR378
CARG416
CTHR472

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY C 507
ChainResidue
CILE75
CGLN226
CMET227
CASP228
CARG229

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

220472

PDB entries from 2024-05-29

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