Structure of PDB 8c53 Chain B

Receptor sequence
>8c53B (length=447) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
NTNLRTKTLRDGTTAEELFSQDGLSFNDFIILPGFIDFDSSKVNVSGQFT
KNILLHLPLVSSPMDTVTESSMARAMALMGGIGVIHNNCTVEQQARMVRS
VKLYRNGFIMKPKSVSPDVPVSTIRNIKSEKGISGILVTEGGKYDGKLLG
IVCTKDIDFVKDASAPVSQYMTRRENMTVERYPIKLEEAMDVLNRSRHGY
LPVLNDKDEVVCLCSRRDAVRARDYPNSSLDRNGHLLCAAATSTREADKG
RVAALSEAGIDVLVLDSSQGNTIYQVSFIRWVKKTYPHLEVVAGNVVTQD
QAKNLIDAGADSLRIGMGVLACGRPQATAIYKVARYAASRGVPCVADGGL
RNVGDVCKALAVGANVAMLGSMIAGTSETPGEYFFKDGMRLKGAVLDKGS
VLKLLAYIHKGLQQSAQDIGEVSFDAIREKVYEGQVLFNRRSLTAQS
3D structure
PDB8c53 InCellCryst - A streamlined approach to structure elucidation using in cellulo crystallized recombinant proteins
ChainB
Resolution2.3 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 ATP B K157 R199 K155 R197
BS02 GDP B L105 I111 K113 K115 K133 G137 L215 L103 I109 K111 K113 K131 G135 L213
BS03 ATP B C155 D158 T174 M179 T180 H200 G201 Y202 C153 D156 T172 M177 T178 H198 G199 Y200
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
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: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:8c53, PDBe:8c53, PDBj:8c53
PDBsum8c53
PubMed38402242
UniProtP50098|IMDH_TRYBB Inosine-5'-monophosphate dehydrogenase

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