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5UZS

Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and P200

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 Residues21
Detailsbinding site for residue IMP A 500
ChainResidue
AALA47
AGLY338
AMET358
AGLY359
ASER360
ATYR383
AGLY385
AMET386
AGLY387
AGLU411
AGLY412
AMET49
A8L4501
AHOH608
AASN275
AGLY300
ASER301
AILE302
ACYS303
AASP336
AGLY337

site_idAC2
Number of Residues10
Detailsbinding site for residue 8L4 A 501
ChainResidue
AALA248
ATHR305
AGLY387
AVAL409
AGLU411
AIMP500
CPRO25
CSER436
CGLY439
CTYR440

site_idAC3
Number of Residues2
Detailsbinding site for residue PGE A 502
ChainResidue
ALYS6
AASP321

site_idAC4
Number of Residues4
Detailsbinding site for residue PGE A 503
ChainResidue
AASN41
AALA62
AARG63
AGLY65

site_idAC5
Number of Residues3
Detailsbinding site for residue PEG A 504
ChainResidue
ATYR428
AILE431
ALYS435

site_idAC6
Number of Residues21
Detailsbinding site for residue IMP B 500
ChainResidue
BALA47
BMET49
BGLY300
BSER301
BILE302
BCYS303
BASP336
BGLY337
BGLY338
BMET358
BGLY359
BSER360
BTYR383
BGLY385
BMET386
BGLY387
BGLU411
B8L4501
BHOH606
BHOH617
BHOH618

site_idAC7
Number of Residues12
Detailsbinding site for residue 8L4 B 501
ChainResidue
APRO25
ASER436
AGLY439
ATYR440
BALA248
BTHR305
BMET386
BGLY387
BMET392
BVAL409
BGLU411
BIMP500

site_idAC8
Number of Residues5
Detailsbinding site for residue PEG B 502
ChainResidue
BASN41
BARG63
BGLU64
BGLY65
BHOH601

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO B 503
ChainResidue
BILE4
BLYS6
BTHR7

site_idAD1
Number of Residues3
Detailsbinding site for residue PGE B 504
ChainResidue
BLYS6
BTHR317
BASP321

site_idAD2
Number of Residues4
Detailsbinding site for residue MG B 505
ChainResidue
BGLU366
BGLU366
BHIS422
BHIS422

site_idAD3
Number of Residues6
Detailsbinding site for residue K B 506
ChainResidue
BGLU465
BSER466
BHIS467
DGLY298
DGLY300
DCYS303

site_idAD4
Number of Residues22
Detailsbinding site for residue IMP C 500
ChainResidue
CCYS303
CASP336
CGLY337
CGLY338
CGLY359
CSER360
CTYR383
CGLY385
CMET386
CGLY387
CGLU411
CGLY412
C8L4501
CHOH605
CHOH607
CHOH610
CHOH631
CALA47
CMET49
CGLY300
CSER301
CILE302

site_idAD5
Number of Residues13
Detailsbinding site for residue 8L4 C 501
ChainResidue
CALA248
CTHR305
CMET386
CGLY387
CPHE408
CVAL409
CGLU411
CIMP500
CHOH602
DPRO25
DSER436
DGLY439
DTYR440

site_idAD6
Number of Residues5
Detailsbinding site for residue PEG C 502
ChainResidue
CASN41
CALA62
CARG63
CGLU64
CGLY65

site_idAD7
Number of Residues3
Detailsbinding site for residue PGE C 503
ChainResidue
CLYS6
CASP321
CHOH608

site_idAD8
Number of Residues2
Detailsbinding site for residue EDO C 504
ChainResidue
CILE4
CTHR7

site_idAD9
Number of Residues7
Detailsbinding site for residue PGE C 505
ChainResidue
ALYS407
APHE408
AHOH615
CTYR428
CILE431
CGLY432
CLYS435

site_idAE1
Number of Residues6
Detailsbinding site for residue K C 506
ChainResidue
CGLY298
CGLY300
CCYS303
DGLU465
DSER466
DHIS467

site_idAE2
Number of Residues23
Detailsbinding site for residue IMP D 500
ChainResidue
DALA47
DASN275
DGLY300
DSER301
DILE302
DCYS303
DASP336
DGLY337
DGLY338
DMET358
DGLY359
DSER360
DTYR383
DGLY385
DMET386
DGLY387
DGLU411
DGLY412
D8L4501
DHOH611
DHOH612
DHOH615
DHOH626

site_idAE3
Number of Residues12
Detailsbinding site for residue 8L4 D 501
ChainResidue
BPRO25
BSER436
BGLY439
BTYR440
DALA248
DTHR305
DMET386
DGLY387
DVAL409
DGLU411
DIMP500
DHOH606

site_idAE4
Number of Residues4
Detailsbinding site for residue PEG D 502
ChainResidue
CPHE408
DTYR428
DGLY432
DLYS435

site_idAE5
Number of Residues3
Detailsbinding site for residue PEG D 503
ChainResidue
DILE4
DLYS6
DTHR7

site_idAE6
Number of Residues4
Detailsbinding site for residue PEG D 504
ChainResidue
DASN41
DARG63
DGLU64
DGLY65

site_idAE7
Number of Residues5
Detailsbinding site for residue PG4 D 505
ChainResidue
BVAL17
DLEU5
DLYS6
DTHR317
DASP321

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT
ChainResidueDetails
AVAL293-THR305

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PDB entries from 2024-07-24

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