Structure of PDB 4ad6 Chain B

Receptor sequence
>4ad6B (length=160) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
SHMIQAYLGLGSNIGDRESQLNDAIKILNEYDGISVSNISPIYETAPVGY
TEQPNFLNLCVEIQTTLTVLQLLECCLKTEECLHRIRKERWGPRTLDVDI
LLYGEEMIDLPKLSVPHPRMNERAFVLIPLNDIAANVVEPRSKLKVKDLV
FVDDSVKRYK
3D structure
PDB4ad6 Exploring the Chemical Space Around 8-Mercaptoguanine as a Route to New Inhibitors of the Folate Biosynthesis Enzyme Hppk.
ChainB
Resolution1.85 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) R85 R94 D97 D99
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 GSY B P109 K110 P111 K112 MOAD: Kd=16.7uM
BS02 GSY B T43 A44 V46 F54 N56 D95 F123 T45 A46 V48 F56 N58 D97 F125 MOAD: Kd=16.7uM
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:4ad6, PDBe:4ad6, PDBj:4ad6
PDBsum4ad6
PubMed23565155
UniProtA0A0H3JKY1

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