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6MGU

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus Anthracis in the complex with inhibitor Oxanosine monophosphate

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
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue JQS A 500
ChainResidue
AALA49
AGLY342
AGLY343
AMET362
AGLY364
ASER365
ATYR388
AGLY390
AMET391
AGLY392
AGLU416
AMET51
AGLY417
AHOH626
AHOH633
AHOH640
AHOH670
AHOH679
AASN280
AGLY305
ASER306
AILE307
ACYS308
ATHR310
AASP341

site_idAC2
Number of Residues6
Detailsbinding site for residue K A 501
ChainResidue
AGLY303
AGLY305
ACYS308
AGLU470
ASER471
AHIS472

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 502
ChainResidue
APHE6
AGLU9
ALEU11
ATHR322
AHOH651

site_idAC4
Number of Residues5
Detailsbinding site for residue PGE A 503
ChainResidue
ASER39
AARG268
APRO272
ASER273
AASN275

site_idAC5
Number of Residues5
Detailsbinding site for residue PEG A 504
ChainResidue
AGLY10
ALEU11
AASP15
AMET463
AHOH700

site_idAC6
Number of Residues5
Detailsbinding site for residue PEG A 505
ChainResidue
APRO27
AHIS254
AGLU416
AALA441
AGLY444

site_idAC7
Number of Residues22
Detailsbinding site for residue JQS B 500
ChainResidue
BALA49
BGLY305
BSER306
BILE307
BCYS308
BTHR310
BASP341
BGLY342
BGLY343
BMET362
BGLY364
BSER365
BTYR388
BGLY390
BMET391
BGLY392
BGLU416
BGLY417
BHOH625
BHOH636
BHOH644
BHOH655

site_idAC8
Number of Residues6
Detailsbinding site for residue K B 501
ChainResidue
BGLY303
BGLY305
BCYS308
BGLU470
BSER471
BHIS472

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO B 502
ChainResidue
BPHE6
BTHR322
BHOH630

site_idAD1
Number of Residues5
Detailsbinding site for residue PEG B 503
ChainResidue
BSER39
BARG268
BPRO272
BSER273
BASN275

site_idAD2
Number of Residues5
Detailsbinding site for residue PEG B 504
ChainResidue
BGLY10
BLEU11
BMET463
BHOH661
BHOH666

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 2026-01-14

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