Structure of PDB 1zfj Chain A

Receptor sequence
>1zfjA (length=476) Species: 1314 (Streptococcus pyogenes) [Search protein sequence]
SNWDTKFLKKGYTFDDVLLIPAESHVLPNEVDLKTKLADNLTLNIPIITA
AMDTVTGSKMAIAIARAGGLGVIHKNMSITEQAEEVRKVKRSENGVIIDP
FFLTPEHKVSEAEELMQRYRISGVPIVETLANRKLVGIITNRDMRFISDY
NAPISEHMTSEHLVTAAVGTDLETAERILHEHRIEKLPLVDNSGRLSGLI
TIKDIEKVIEFPHAAKDEFGRLLVAAAVGVTSDTFERAEALFEAGADAIV
IDTAHGHSAGVLRKIAEIRAHFPNRTLIAGNIATAEGARALYDAGVDVVK
VGIGPGSICTTRVVAGVGVPQVTAIYDAAAVAREYGKTIIADGGIKYSGD
IVKALAAGGNAVMLGSMFAGTDEAPGETEIYQGRKYKTYRGMGSIAAMKK
NKLVPEGIEGRVAYKGAASDIVFQMLGGIRSGMGYVGAGDIQELHENAQF
VEMSGAGLIESHPHDVQITNEAPNYS
3D structure
PDB1zfj Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase.
ChainA
Resolution1.9 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 M53 G307 S308 I309 C310 D343 G366 S367 Y390 G392 M393 G394 E486 S491 M52 G306 S307 I308 C309 D342 G365 S366 Y389 G391 M392 G393 E471 S476
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:1zfj, PDBe:1zfj, PDBj:1zfj
PDBsum1zfj
PubMed10200156
UniProtP0C0H6|IMDH_STRPY Inosine-5'-monophosphate dehydrogenase (Gene Name=guaB)

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