Structure of PDB 7qdx Chain B

Receptor sequence
>7qdxB (length=403) Species: 83333,208964 [Search protein sequence]
RIAKEALTFDDVLLVPAHSTVLPNTADLSTQLTKTIRLNIPMLSAAMDTV
TEARLAIALAQEGGIGFIHKNMSIERQAEEVRRVKKHESAIVRDPVTVTP
STKIIELLQMAREYGFSGFPVVEQGELVGIVTGRDLRVKDTVAAIMTPKD
KLVTAREGTPLEEMKAKLYENRIEKMLVVDENFYLRGLVTFRDIEKAERK
PNACKDEQGRLRVGAAVGAGAGNEERVDALVAAGVDVLLIDSSHGHSEGV
LQRIRETRAKYPDLQIIGGNVATAAGARALAEAGCSAVKVGIGPCTTRIV
TGVGVPQITAVADAVEALEGTGIPVIADGGIRFSGDIAKAIAAGASAVMV
GSMLAGTEESPYKGRLKEIIHQQMGGLRSCMGLTGCGTIDELRTKAEFVR
ISG
3D structure
PDB7qdx Insight into the role of the Bateman domain at the molecular and physiological levels through engineered IMP dehydrogenases.
ChainB
Resolution2.9 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 ATP B I152 T154 G155 R156 D157 T173 L178 V179 I199 E200 K201 I130 T132 G133 R134 D135 T147 L152 V153 I173 E174 K175
BS02 ATP B V118 F138 G140 E200 K201 T216 R218 D219 V96 F116 G118 E174 K175 T190 R192 D193
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:7qdx, PDBe:7qdx, PDBj:7qdx
PDBsum7qdx
PubMed37338125
UniProtP0ADG7;
Q9HXM5

[Back to BioLiP]