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5VSV

Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and P225

Replaces:  5UZO
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 Residues26
Detailsbinding site for residue IMP A 501
ChainResidue
AALA47
AGLY337
AGLY338
AMET357
AMET358
AGLY359
ASER360
ATYR383
AGLY385
AMET386
AGLY387
AMET49
AGLU411
AGLY412
A8KY502
AHOH613
AHOH629
AHOH642
AHOH643
AASN275
AGLY300
ASER301
AILE302
ACYS303
ATHR305
AASP336

site_idAC2
Number of Residues12
Detailsbinding site for residue 8KY A 502
ChainResidue
ATHR247
AALA248
AHIS249
AGLY387
AVAL409
AGLU411
AIMP501
AHOH623
CPRO25
CSER436
CGLY439
CTYR440

site_idAC3
Number of Residues13
Detailsbinding site for residue 8KY A 503
ChainResidue
AVAL23
APRO25
ASER436
AGLY439
ATYR440
BTHR247
BHIS249
BTHR305
BMET386
BGLY387
BVAL409
BGLU411
BIMP500

site_idAC4
Number of Residues25
Detailsbinding site for residue IMP B 500
ChainResidue
A8KY503
BALA47
BMET49
BASN275
BGLY300
BSER301
BILE302
BCYS303
BTHR305
BASP336
BGLY337
BGLY338
BMET358
BGLY359
BSER360
BTYR383
BGLY385
BMET386
BGLY387
BGLU411
BGLY412
BHOH601
BHOH604
BHOH610
BHOH638

site_idAC5
Number of Residues11
Detailsbinding site for residue 8KY B 501
ChainResidue
BPRO25
BSER436
BGLY439
BTYR440
DTHR247
DALA248
DHIS249
DMET386
DVAL409
DGLU411
DIMP500

site_idAC6
Number of Residues23
Detailsbinding site for residue IMP C 500
ChainResidue
CTYR383
CGLY385
CMET386
CGLY387
CGLU411
CGLY412
C8KY501
CHOH601
CHOH606
CHOH607
CHOH618
CALA47
CMET49
CASN275
CGLY300
CSER301
CCYS303
CASP336
CGLY337
CGLY338
CMET358
CGLY359
CSER360

site_idAC7
Number of Residues12
Detailsbinding site for residue 8KY C 501
ChainResidue
CTHR247
CALA248
CHIS249
CTHR305
CMET386
CGLY387
CVAL409
CGLU411
CIMP500
DPRO25
DSER436
DTYR440

site_idAC8
Number of Residues25
Detailsbinding site for residue IMP D 500
ChainResidue
B8KY501
DALA47
DMET49
DASN275
DGLY300
DSER301
DILE302
DCYS303
DTHR305
DASP336
DGLY337
DGLY338
DMET357
DMET358
DGLY359
DSER360
DTYR383
DGLY385
DMET386
DGLY387
DGLU411
DGLY412
DHOH603
DHOH619
DHOH626

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

223532

PDB entries from 2024-08-07

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