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5UPU

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Mycobacterium tuberculosis in the presence of TBK6

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0006164biological_processpurine nucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue IMP A 601
ChainResidue
ASER83
ASER398
ATYR421
AGLY423
AMET424
AGLY425
AGLU458
AGLY459
A6Q9602
AMET85
ASER339
AILE340
ACYS341
AASP374
AGLY375
AGLY376
AGLY397

site_idAC2
Number of Residues9
Detailsbinding site for residue 6Q9 A 602
ChainResidue
AASP283
AALA285
AGLY334
AVAL335
AGLY336
ATHR343
AMET424
AGLY425
AIMP601

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGVGpGSICtT
ChainResidueDetails
AVAL331-THR343

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000305|PubMed:26440283
ChainResidueDetails
ACYS341

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000305|PubMed:26440283
ChainResidueDetails
AARG443

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:26440283
ChainResidueDetails
AASP283
ASER339
AASP374
AGLY397
ATYR421
AGLU511
ASER512
AHIS513

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:26440283
ChainResidueDetails
AASN289
ATHR343
AGLU458

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01964
ChainResidueDetails
AGLY334

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:26440283
ChainResidueDetails
AGLY336
AGLY338
ACYS341

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PDB entries from 2024-07-24

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