Structure of PDB 6rfu Chain B

Receptor sequence

>6rfuB (length=448) Species: 5702 (Trypanosoma brucei brucei)

NTNLRTKTLRDGTTAEELFSQDGLSFNDFIILPGFIDFDSSKVNVSGQFT
KNILLHLPLVSSPMDTVTESSMARAMALMGGIGVIHNNCTVEQQARMVRS
VKLYRNGFIMKPKSVSPDVPVSTIRNIKSEKGISGILVTEGGKYDGKLLG
IVCTKDIDFVKDASAPVSQYMTRRENMTVERYPIKLEEAMDVLNRSRHGY
LPVLNDKDEVVCLCSRRDAVRARDYPNSSLDRNGHLLCAAATSTREADKG
RVAALSEAGIDVLVLDSSQGNTIYQVSFIRWVKKTYPHLEVVAGNVVTQD
QAKNLIDAGADSLRIGMGLACGRPQATAIYKVARYAASRGVPCVADGGLR
NVGDVCKALAVGANVAMLGSMIAGTSETPGEYFFKDGMRLKGGAVLDKGS
VLKLLAYIHKGLQQSAQDIGEVSFDAIREKVYEGQVLFNRRTLTAQSE

3D structure

• PDB: 6rfu In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors.
• Chain: B
• Resolution: 2.8 Å

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	ATP	B	S136 C155 T156 D158 T174 M179 T180 H200 G201 Y202 R219	S134 C153 T154 D156 T172 M177 T178 H198 G199 Y200 R217
BS03	5GP	B	I111 K113 P114 K115 K133 I135 L215	I109 K111 P112 K113 K131 I133 L213

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

External links

• PDB: RCSB:6rfu, PDBe:6rfu, PDBj:6rfu
• PDBsum: 6rfu
• PubMed: 32001697
• UniProt: P50098|IMDH_TRYBB Inosine-5'-monophosphate dehydrogenase