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7QDX

bacterial IMPDH chimera

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 PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT
ChainResidueDetails
AVAL314-THR326

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_01964
ChainResidueDetails
ACYS324
BCYS324

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01964
ChainResidueDetails
AARG420
BARG420

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01964
ChainResidueDetails
AASP267
AHIS490
BASP267
BGLY317
BSER322
BASP357
BGLY380
BTYR404
BGLU434
BGLU488
BSER489
AGLY317
BHIS490
ASER322
AASP357
AGLY380
ATYR404
AGLU434
AGLU488
ASER489

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01964
ChainResidueDetails
AGLY319
AGLY321
ACYS324
BGLY319
BGLY321
BCYS324

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS286
ALYS447
BLYS286
BLYS447

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PDB entries from 2024-07-24

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