Structure of PDB 5ou2 Chain A

Receptor sequence
>5ou2A (length=330) Species: 1078020 (Mycolicibacterium thermoresistibile ATCC 19527) [Search protein sequence]
VPTGGDDPTKIAMLGLTFDDVLLLPAASDVLPANADTSSQLTKKIRLKVP
LVSSAMDTVTEARMAIAMARAGGMGVLHRNLPVAEQAAQVETVKRSGGLL
VGAAVGVGDDAWERAMALRDAGVDVLVVDTAHAHNRKVLDMVHRLKTTVG
DEIEVVGGNVATRAAAAALVEAGADAVKVGVGPGSICTTRVVAGVGAPQI
TAILEAVAACAPHGVPVIADGGLQYSGDIAKALAAGASTAMLGSLLAGTA
ESPGELILVNGKQFKSYRGMGSLGAMQVPEGIEGRVPFRGPLSTVIHQLV
GGLRAAMGYTGSATIEELQQAQFVQITAAG
3D structure
PDB5ou2 Fragment-Based Approach to Targeting Inosine-5'-monophosphate Dehydrogenase (IMPDH) from Mycobacterium tuberculosis.
ChainA
Resolution1.45 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 S54 M56 G184 S185 I186 C187 D220 G222 G243 S244 Y267 G269 M270 G271 E280
BS02 36Y A H146 N149 E318 H132 N135 E280 MOAD: Ki=609uM
PDBbind-CN: -logKd/Ki=3.22,Ki=609uM
BS03 36Y A A145 N173 E318 A131 N159 E280 MOAD: Ki=609uM
PDBbind-CN: -logKd/Ki=3.22,Ki=609uM
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5ou2, PDBe:5ou2, PDBj:5ou2
PDBsum5ou2
PubMed29547284
UniProtG7CNL4

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