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6RPU

Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue G5P A 601
ChainResidue
ALYS115
AARG167
AARG167
AASP168
ATHR184
AASP186
AVAL187
AILE188
AGLY209
ALYS210
APRO212
ATYR116
AMET223
ASER225
ATHR227
AASP228
ALYS231
AHOH703
APRO124
AVAL125
APHE145
AALA146
AGLY147
ATHR165
ASER166

site_idAC2
Number of Residues9
Detailsbinding site for residue GDP A 602
ChainResidue
AGLU117
AASN118
AGLY119
AASN200
AASP228
ALEU229
AASN232
ALYS240
ALYS245

site_idAC3
Number of Residues4
Detailsbinding site for residue ACT A 603
ChainResidue
AGLY368
AGLY369
AGLY390
AGLY391

site_idAC4
Number of Residues2
Detailsbinding site for residue ACT A 604
ChainResidue
ASER278
ASER279

site_idAC5
Number of Residues1
Detailsbinding site for residue ACT A 605
ChainResidue
ASER234

site_idAC6
Number of Residues1
Detailsbinding site for residue ACT A 606
ChainResidue
ASER494

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRIGMGsGSICiT
ChainResidueDetails
ALEU324-THR336

226707

PDB entries from 2024-10-30

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