Structure of PDB 6lk4 Chain A

Receptor sequence
>6lk4A (length=424) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
FNESASIPTGLTYDDVLIIPQHSRVTSRKEVNTTTRLSRNVKLSIPIVAS
NMDTVCEQRMAVAMAREGGIGILHRFCSIEEQCAMLREVKRAQSFLIESP
RIILPHETAREAWEGLNWKGRVGGVGCLLVVNCKNERKLLGIITRHDLKL
ADESTTVESLMTPVDKMVVSTNTSISLEEVTHLMRKGRTANVPIVGQNGQ
LLYLVTLSDVVKLRKNKQASLDSRGRLLVGAAVGVKKDDMNRAIRLVEAG
ADVLVVDIAHGHSDLCINMVKRLKGDPRTASVDIIAGNIASAEAAEALID
AGADGLKIGVGPGSICITRLVAGAGVPQLSAVLACTRVARRRGVPCIADG
GLRTSGDISKAIGAGADTVMLGNMLAGTDEAPCKGPVGPIVRQLVGGLRS
GMSYSGAKSIEEMQRRTRFVRMTG
3D structure
PDB6lk4 Allosteric regulation accompanied by oligomeric state changes of Trypanosoma brucei GMP reductase through cystathionine-beta-synthase domain.
ChainA
Resolution2.503 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 GTP A R93 I99 P102 R103 R123 V127 G128 C129 L206 S210 D211 K214 R91 I97 P100 R101 R121 V125 G126 C127 L204 S208 D209 K212 MOAD: Kd=6.75uM
BS02 PO4 A G352 N375 G350 N373
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:6lk4, PDBe:6lk4, PDBj:6lk4
PDBsum6lk4
PubMed32296055
UniProtQ57ZS7

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