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6RFU

In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of ATP and GMP as genuine co-factors

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0020015cellular_componentglycosome
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0005737cellular_componentcytoplasm
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006183biological_processGTP biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0020015cellular_componentglycosome
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue ATP A 601
ChainResidue
ASER136
AHIS200
AGLY201
ATYR202
AARG219
BLYS157
BARG199
ACYS155
ATHR156
ALYS157
AASP158
ATHR174
AASN178
AMET179
ATHR180

site_idAC2
Number of Residues10
Detailsbinding site for residue 5GP A 602
ChainResidue
ALEU105
AILE111
AMET112
ALYS113
ALYS115
ALYS133
ASER136
AGLY137
ATYR202
ALEU215

site_idAC3
Number of Residues13
Detailsbinding site for residue ATP B 601
ChainResidue
ALYS157
AARG199
BSER136
BCYS155
BTHR156
BASP158
BTHR174
BMET179
BTHR180
BHIS200
BGLY201
BTYR202
BARG219

site_idAC4
Number of Residues9
Detailsbinding site for residue 5GP B 602
ChainResidue
BILE111
BLYS113
BPRO114
BLYS115
BLYS133
BILE135
BSER136
BGLY137
BLEU215

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRIGMGsGSICiT
ChainResidueDetails
ALEU315-THR327

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
ACYS325
BCYS325

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AARG423
BARG423

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AASP268
BASP268
BGLY318
BSER323
BASP358
BGLY381
BTYR405
BGLN435
BGLU494
BGLY495
AGLY318
ASER323
AASP358
AGLY381
ATYR405
AGLN435
AGLU494
AGLY495

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AGLY320
AGLY322
ACYS325
BGLY320
BGLY322
BCYS325

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PDB entries from 2024-09-04

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