Structure of PDB 8c53 Chain A

Receptor sequence
>8c53A (length=448) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
NTNLRTKTLRDGTTAEELFSQDGLSFNDFIILPGFIDFDSSKVNVSGQFT
KNILLHLPLVSSPMDTVTESSMARAMALMGGIGVIHNNCTVEQQARMVRS
VKLYRNGFIMKPKSVSPDVPVSTIRNIKSEKGISGILVTEGGKYDGKLLG
IVCTKDIDFVKDASAPVSQYMTRRENMTVERYPIKLEEAMDVLNRSRHGY
LPVLNDKDEVVCLCSRRDAVRARDYPNSSLDRNGHLLCAAATSTREADKG
RVAALSEAGIDVLVLDSSQGNTIYQVSFIRWVKKTYPHLEVVAGNVVTQD
QAKNLIDAGADSLRIGMGSVLACGRPQATAIYKVARYAASRGVPCVADGG
LRNVGDVCKALAVGANVAMLGSMIAGTSETPGEYFFKDGMRLKGAVLDKG
SVLKLLAYIHKGLQQSAQDIGEVSFDAIREKVYEGQVLFNRRSLTAQS
3D structure
PDB8c53 InCellCryst - A streamlined approach to structure elucidation using in cellulo crystallized recombinant proteins
ChainA
Resolution2.3 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 GDP A L105 I111 K113 K115 K133 S136 G137 L103 I109 K111 K113 K131 S134 G135
BS02 ATP A I153 C155 D158 T174 M179 T180 H200 G201 Y202 R219 I151 C153 D156 T172 M177 T178 H198 G199 Y200 R217
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8c53, PDBe:8c53, PDBj:8c53
PDBsum8c53
PubMed38402242
UniProtP50098|IMDH_TRYBB Inosine-5'-monophosphate dehydrogenase

[Back to BioLiP]