Structure of PDB 3qbc Chain B

Receptor sequence
>3qbcB (length=161) Species: 158878 (Staphylococcus aureus subsp. aureus Mu50) [Search protein sequence]
GSHMIQAYLGLGSNIGDRESQLNDAIKILNEYDGISVSNISPIYETAPVG
YTEQPNFLNLCVEIQTTLTVLQLLECCLKTEECLHRIRKERWGPRTLDVD
ILLYGEEMIDLPKLSVPHPRMNERAFVLIPLNDIAANVVEPRSKLKVKDL
VFVDDSVKRYK
3D structure
PDB3qbc Structure of S. aureus HPPK and the discovery of a new substrate site inhibitor
ChainB
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R83 R92 D95 D97
Catalytic site (residue number reindexed from 1) R86 R95 D98 D100
Enzyme Commision number 2.7.6.3: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.
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 B55 B P109 K110 P112 K113 MOAD: Kd=10.8uM
BS02 B55 B T43 A44 V46 F54 N56 F123 T46 A47 V49 F57 N59 F126 MOAD: Kd=10.8uM
Gene Ontology
Molecular Function
GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0016310 phosphorylation
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3qbc, PDBe:3qbc, PDBj:3qbc
PDBsum3qbc
PubMed22276115
UniProtA0A0H3JXR3

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