Structure of PDB 5ou3 Chain A

Receptor sequence
>5ou3A (length=333) Species: 1078020 (Mycolicibacterium thermoresistibile ATCC 19527) [Search protein sequence]
PVPTGGDDPTKIAMLGLTFDDVLLLPAASDVLPANADTSSQLTKKIRLKV
PLVSSAMDTVTEARMAIAMARAGGMGVLHRNLPVAEQAAQVETVKRSGGL
LVGAAVGVGDDAWERAMALRDAGVDVLVVDTAHAHNRKVLDMVHRLKTTV
GDEIEVVGGNVATRAAAAALVEAGADAVKVGVGPGSICTTRVVAGVGAPQ
ITAILEAVAACAPHGVPVIADGGLQYSGDIAKALAAGASTAMLGSLLAGT
AESPGELILVNGKQFKSYRGMGSLGAMQGVPEGIEGRVPFRGPLSTVIHQ
LVGGLRAAMGYTGSATIEELQQAQFVQITAAGL
3D structure
PDB5ou3 Fragment-Based Approach to Targeting Inosine-5'-monophosphate Dehydrogenase (IMPDH) from Mycobacterium tuberculosis.
ChainA
Resolution1.6 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 IMP A S68 M70 G198 S199 I200 C201 D234 G236 G257 S258 Y281 G283 M284 G285 E318 S55 M57 G185 S186 I187 C188 D221 G223 G244 S245 Y268 G270 M271 G272 E282
BS02 AUN A D143 H146 N173 G285 E318 D130 H133 N160 G272 E282 MOAD: Ki=0.61uM
PDBbind-CN: -logKd/Ki=6.21,Ki=0.61uM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5ou3, PDBe:5ou3, PDBj:5ou3
PDBsum5ou3
PubMed29547284
UniProtG7CNL4

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