Structure of PDB 6jig Chain A

Receptor sequence
>6jigA (length=480) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
FNESASIPTGLTYDDVLIIPQHSRVTSRKEVNTTTRLSRNVKLSIPIVAS
NMDTVCEQRMAVAMAREGGIGILHRFCSIEEQCAMLREVKRAQSFLIESP
RIILPHETAREAWEGLNWKGRVGGVGCLLVVNCKNERKLLGIITRHDLKL
ADESTTVESLMTPVDKMVVSTNTSISLEEVTHLMRKGRTANVPIVGQNGQ
LLYLVTLSDVVKLRKNKQASLDSRGRLLVGAAVGVKKDDMNRAIRLVEAG
ADVLVVDIAHGHSDLCINMVKRLKGDPRTASVDIIAGNIASAEAAEALID
AGADGLKIGVGPGSIAITRLVAGAGVPQLSAVLACTRVARRRGVPCIADG
GLRTSGDISKAIGAGADTVMLGNMLAGTDEAPGRVLVKDGQKVKIIRGMA
GFGANLSKAERERTSLVPEGVEGSVACKGPVGPIVRQLVGGLRSGMSYSG
AKSIEEMQRRTRFVRMTGAGLRESGSHGVA
3D structure
PDB6jig Allosteric regulation accompanied by oligomeric state changes of Trypanosoma brucei GMP reductase through cystathionine-beta-synthase domain.
ChainA
Resolution1.903 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 5GP A S52 G315 S316 I317 A318 T320 D351 G374 N375 G400 M401 A402 E428 S50 G313 S314 I315 A316 T318 D349 G372 N373 G398 M399 A400 E419
BS02 5GP A R93 Q95 I99 P102 R103 R123 V127 G128 C129 D211 R91 Q93 I97 P100 R101 R121 V125 G126 C127 D209
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003920 GMP reductase activity
GO:0003938 IMP dehydrogenase activity
GO:0005525 GTP binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006183 GTP biosynthetic process
Cellular Component
GO:0005730 nucleolus
GO:0005737 cytoplasm
GO:0020015 glycosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6jig, PDBe:6jig, PDBj:6jig
PDBsum6jig
PubMed32296055
UniProtQ57ZS7

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