Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5UWX

Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and P176

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 Residues14
Detailsbinding site for residue 8L7 A 500
ChainResidue
AALA248
BLEU24
BPRO25
BSER436
BGLY439
BTYR440
ASER252
AGLY254
ATHR305
AMET386
AGLY387
AGLU411
AIMP501
AHOH681

site_idAC2
Number of Residues26
Detailsbinding site for residue IMP A 501
ChainResidue
AALA47
AMET49
AASN275
AGLY300
ASER301
AILE302
ACYS303
AASP336
AGLY337
AGLY338
AMET357
AMET358
AGLY359
ASER360
ATYR383
AGLY385
AMET386
AGLY387
AGLU411
AGLY412
A8L7500
AHOH613
AHOH632
AHOH637
AHOH696
AHOH708

site_idAC3
Number of Residues4
Detailsbinding site for residue MPD A 502
ChainResidue
ALYS6
AALA277
AGLU280
AASP321

site_idAC4
Number of Residues2
Detailsbinding site for residue ACY A 503
ChainResidue
ALYS340
AHOH698

site_idAC5
Number of Residues15
Detailsbinding site for residue 8L7 B 500
ChainResidue
BVAL224
BTHR247
BHIS249
BSER252
BGLY254
BTHR305
BMET386
BGLY387
BMET392
BGLU411
BIMP501
BHOH619
CSER436
CGLY439
CTYR440

site_idAC6
Number of Residues25
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
B8L7500
BHOH610
BHOH616
BHOH681
BHOH688
BHOH699

site_idAC7
Number of Residues3
Detailsbinding site for residue MPD B 502
ChainResidue
BLYS6
BALA277
BASP321

site_idAC8
Number of Residues3
Detailsbinding site for residue MRD B 503
ChainResidue
BLYS340
BSER481
BHOH602

site_idAC9
Number of Residues18
Detailsbinding site for residue 8L7 C 500
ChainResidue
CGLY387
CMET392
CGLU411
CIMP501
CHOH681
DVAL23
DLEU24
DPRO25
DSER436
DGLY439
DTYR440
CTHR247
CALA248
CHIS249
CSER252
CGLY254
CTHR305
CMET386

site_idAD1
Number of Residues25
Detailsbinding site for residue IMP C 501
ChainResidue
CALA47
CMET49
CASN275
CGLY300
CSER301
CILE302
CCYS303
CASP336
CGLY337
CGLY338
CMET358
CGLY359
CSER360
CTYR383
CGLY385
CMET386
CGLY387
CGLU411
CGLY412
C8L7500
CHOH606
CHOH646
CHOH648
CHOH667
CHOH670

site_idAD2
Number of Residues2
Detailsbinding site for residue ACY C 502
ChainResidue
CLYS340
CHOH663

site_idAD3
Number of Residues4
Detailsbinding site for residue MPD C 503
ChainResidue
CLYS6
CALA277
CPRO279
CASP321

site_idAD4
Number of Residues15
Detailsbinding site for residue 8L7 D 500
ChainResidue
ALEU24
ASER436
AGLY439
ATYR440
DVAL224
DALA248
DHIS249
DSER252
DLYS253
DGLY254
DTHR305
DMET386
DGLY387
DGLU411
DIMP501

site_idAD5
Number of Residues25
Detailsbinding site for residue IMP D 501
ChainResidue
DALA47
DMET49
DASN275
DGLY300
DSER301
DILE302
DCYS303
DASP336
DGLY337
DGLY338
DMET358
DGLY359
DSER360
DTYR383
DGLY385
DMET386
DGLY387
DGLU411
DGLY412
D8L7500
DHOH603
DHOH618
DHOH635
DHOH638
DHOH641

site_idAD6
Number of Residues4
Detailsbinding site for residue MPD D 502
ChainResidue
DLYS6
DALA277
DPRO279
DASP321

site_idAD7
Number of Residues2
Detailsbinding site for residue ACY D 503
ChainResidue
DASN479
DHOH602

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

251801

PDB entries from 2026-04-08

PDB statisticsPDBj update infoContact PDBjnumon