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5UZC

Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and P221

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
AALA47
AGLY338
AMET358
AGLY359
ASER360
ATYR383
AGLY385
AMET386
AGLY387
AGLU411
AGLY412
AMET49
A8N1502
AHOH606
AHOH616
AHOH663
AHOH681
AHOH694
AASN275
AGLY300
ASER301
AILE302
ACYS303
AASP336
AGLY337

site_idAC2
Number of Residues15
Detailsbinding site for residue 8N1 A 502
ChainResidue
ATHR247
AALA248
AHIS249
ASER252
ATHR305
AMET386
AGLY387
AMET392
AGLU411
AIMP501
AHOH601
DLEU24
DSER436
DGLY439
DTYR440

site_idAC3
Number of Residues4
Detailsbinding site for residue MPD A 503
ChainResidue
ALYS6
AALA277
APRO279
AASP321

site_idAC4
Number of Residues2
Detailsbinding site for residue ACY A 504
ChainResidue
ALYS340
AHOH696

site_idAC5
Number of Residues4
Detailsbinding site for residue FMT A 505
ChainResidue
ASER460
BSER460
CSER460
DSER460

site_idAC6
Number of Residues24
Detailsbinding site for residue IMP B 501
ChainResidue
BALA47
BMET49
BASN275
BGLY300
BSER301
BILE302
BCYS303
BASP336
BGLY337
BGLY338
BMET358
BGLY359
BSER360
BTYR383
BGLY385
BMET386
BGLY387
BGLU411
BGLY412
B8N1502
BHOH619
BHOH665
BHOH676
BHOH684

site_idAC7
Number of Residues16
Detailsbinding site for residue 8N1 B 502
ChainResidue
ALEU24
APRO25
ASER436
AGLY439
ATYR440
BTHR247
BALA248
BHIS249
BSER252
BVAL255
BTHR305
BMET386
BGLY387
BGLU411
BIMP501
BHOH688

site_idAC8
Number of Residues2
Detailsbinding site for residue MPD B 503
ChainResidue
BALA277
BASP321

site_idAC9
Number of Residues3
Detailsbinding site for residue FMT B 504
ChainResidue
BLYS340
BLYS420
BHOH658

site_idAD1
Number of Residues24
Detailsbinding site for residue IMP C 500
ChainResidue
CSER301
CILE302
CCYS303
CASP336
CGLY337
CGLY338
CMET358
CGLY359
CSER360
CTYR383
CGLY385
CMET386
CGLY387
CGLU411
CGLY412
C8N1501
CHOH612
CHOH623
CHOH638
CHOH646
CALA47
CMET49
CASN275
CGLY300

site_idAD2
Number of Residues20
Detailsbinding site for residue 8N1 C 501
ChainResidue
BLEU24
BPRO25
BSER436
BGLY439
BTYR440
CVAL224
CTHR247
CALA248
CHIS249
CSER252
CGLY254
CVAL255
CTHR305
CMET386
CGLY387
CMET392
CGLU411
CIMP500
CHOH601
CHOH648

site_idAD3
Number of Residues3
Detailsbinding site for residue MRD C 502
ChainResidue
CLYS6
CALA277
CASP321

site_idAD4
Number of Residues2
Detailsbinding site for residue ACY C 503
ChainResidue
CLYS340
CHOH656

site_idAD5
Number of Residues25
Detailsbinding site for residue IMP D 500
ChainResidue
DALA47
DMET49
DASN275
DGLY300
DSER301
DILE302
DCYS303
DASP336
DGLY337
DGLY338
DMET358
DGLY359
DSER360
DTYR383
DGLY385
DMET386
DGLY387
DGLU411
DGLY412
D8N1501
DHOH605
DHOH625
DHOH641
DHOH653
DHOH677

site_idAD6
Number of Residues17
Detailsbinding site for residue 8N1 D 501
ChainResidue
CVAL23
CLEU24
CPRO25
CSER436
CGLY439
CTYR440
DTHR247
DALA248
DHIS249
DSER252
DGLY254
DVAL255
DTHR305
DMET386
DGLY387
DGLU411
DIMP500

site_idAD7
Number of Residues3
Detailsbinding site for residue MPD D 502
ChainResidue
DLYS6
DALA277
DASP321

site_idAD8
Number of Residues2
Detailsbinding site for residue ACY D 503
ChainResidue
DLYS340
DHOH664

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

237735

PDB entries from 2025-06-18

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