Structure of PDB 3tsd Chain A

Receptor sequence
>3tsdA (length=442) Species: 198094 (Bacillus anthracis str. Ames) [Search protein sequence]
QSNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPL
ISAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSESGVI
SDPFFLTPEHQVYDAEHLMGKYRISGVPVVNNLDERKLVGIITNRDMRFI
QDYSIKISDVMKEQLITAPVGTTLSEAEKILQKYKIEKLPLVDNNGVLQG
LITIKDIEKVIEFPNSAKDKQGRLLVGAAVGVTADAMTRIDALVKASVDA
IVLDTAHGHSQGVIDKVKEVRAKYPSLNIIAGNVATAEATKALIEAGANV
VKVGIGPGSICTTRVVAGVGVPQLTAVYDCATEARKHGIPVIADGGIKYS
GDMVKALAAGAHVVMLGSMFAGVAESPGERQFKVYRGEGRVPYKGPLADT
VHQLVGGLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHP
3D structure
PDB3tsd Bacillus anthracis inosine 5'-monophosphate dehydrogenase in action: the first bacterial series of structures of phosphate ion-, substrate-, and product-bound complexes.
ChainA
Resolution2.653 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 XMP A M51 G305 S306 I307 C308 D341 G364 S365 Y388 G390 M55 G308 S309 I310 C311 D344 G367 S368 Y385 G387 PDBbind-CN: -logKd/Ki=3.66,Ki=218uM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3tsd, PDBe:3tsd, PDBj:3tsd
PDBsum3tsd
PubMed22788966
UniProtA0A6L8P2U9

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