Structure of PDB 7qem Chain A

Receptor sequence
>7qemA (length=425) Species: 83333,208964 [Search protein sequence]
LRIAKEALTFDDVLLVPAHSTVLPNTADLSTQLTKTIRLNIPMLSAAMDT
VTEARLAIALAQEGGIGFIHKNMSIERQAEEVRRVKKHESAIVRDPVTVT
PSTKIIELLQMAREYGFSGFPVVEQGELVGIVTGRDLRVKPDTVAAIMTP
KDKLVTAREGTPLEEMKAKLYENRIEKMLVVDENFYLRGLVTFRDIEKAE
RKPNACKDEQGRLRVGAAVGAGAGNEERVDALVAAGVDVLLIDSSHGHSE
GVLQRIRETRAKYPDLQIIGGNVATAAGARALAEAGCSAVKVGIGPGSIC
TTRIVTGVGVPQITAVADAVEALEGTGIPVIADGGIRFSGDIAKAIAAGA
SAVMVGSMLAGTEESPGEIELYQGRSYKSYRVAYKGRLKEIIHQQMGGLR
SCMGLTGCGTIDELRTKAEFVRISG
3D structure
PDB7qem Insight into the role of the Bateman domain at the molecular and physiological levels through engineered IMP dehydrogenases.
ChainA
Resolution3.09 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 IMP A S302 D337 G338 G339 S361 S298 D333 G334 G335 S357
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:7qem, PDBe:7qem, PDBj:7qem
PDBsum7qem
PubMed37338125
UniProtP0ADG7;
Q9HXM5

[Back to BioLiP]