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5UUV

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with a product IMP and the inhibitor P182

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 Residues19
Detailsbinding site for residue IMP A 501
ChainResidue
AALA49
AGLY343
ALEU363
AGLY364
ASER365
ATYR388
AGLY390
AMET391
AGLY392
AGLU416
A8L1502
AMET51
AASN280
AGLY305
ASER306
AILE307
ACYS308
AASP341
AGLY342

site_idAC2
Number of Residues13
Detailsbinding site for residue 8L1 A 502
ChainResidue
ATHR252
AALA253
ASER257
AVAL260
ATHR310
AMET391
AVAL414
AGLU416
AIMP501
DLEU26
DALA441
DGLY444
DTYR445

site_idAC3
Number of Residues6
Detailsbinding site for residue K A 503
ChainResidue
AGLY303
AGLY305
ACYS308
DGLU470
DSER471
DHIS472

site_idAC4
Number of Residues6
Detailsbinding site for residue K A 504
ChainResidue
AGLU470
ASER471
AHIS472
CGLY303
CGLY305
CCYS308

site_idAC5
Number of Residues19
Detailsbinding site for residue IMP B 501
ChainResidue
BALA49
BMET51
BASN280
BGLY305
BSER306
BILE307
BCYS308
BASP341
BGLY342
BGLY343
BGLY364
BSER365
BTYR388
BGLY390
BMET391
BGLY392
BGLU416
BGLY417
B8L1502

site_idAC6
Number of Residues10
Detailsbinding site for residue 8L1 B 502
ChainResidue
BTHR252
BSER257
BTHR310
BMET391
BVAL414
BGLU416
BIMP501
CPRO27
CGLY444
CTYR445

site_idAC7
Number of Residues6
Detailsbinding site for residue K B 503
ChainResidue
BGLY303
BGLY305
BCYS308
CGLU470
CSER471
CHIS472

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL B 504
ChainResidue
BPRO272
BSER273
BASN275
BASN296

site_idAC9
Number of Residues6
Detailsbinding site for residue K B 505
ChainResidue
BGLU470
BSER471
BHIS472
DGLY303
DGLY305
DCYS308

site_idAD1
Number of Residues20
Detailsbinding site for residue IMP C 501
ChainResidue
CMET362
CLEU363
CGLY364
CSER365
CTYR388
CGLY390
CMET391
CGLY392
CGLU416
C8L1502
CALA49
CMET51
CASN280
CGLY305
CSER306
CILE307
CCYS308
CASP341
CGLY342
CGLY343

site_idAD2
Number of Residues9
Detailsbinding site for residue 8L1 C 502
ChainResidue
AALA441
AGLY444
CTHR252
CALA253
CSER257
CTHR310
CMET391
CGLU416
CIMP501

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL C 503
ChainResidue
CSER39
CARG268
CSER273
CLEU274
CASN275
CASN296

site_idAD4
Number of Residues19
Detailsbinding site for residue IMP D 500
ChainResidue
DALA49
DMET51
DGLY305
DSER306
DILE307
DCYS308
DTHR310
DASP341
DGLY342
DGLY343
DGLY364
DSER365
DTYR388
DGLY390
DMET391
DGLY392
DGLU416
DGLY417
D8L1501

site_idAD5
Number of Residues12
Detailsbinding site for residue 8L1 D 501
ChainResidue
BLEU26
BGLY444
BTYR445
DVAL229
DTHR252
DALA253
DSER257
DTHR310
DMET391
DVAL414
DGLU416
DIMP500

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT
ChainResidueDetails
AVAL298-THR310

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PDB entries from 2024-11-06

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