Structure of PDB 8sl9 Chain A

Receptor sequence
>8sl9A (length=422) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4) [Search protein sequence]
GMQYIIGIGTNIGFTIENIHLAITALESQQNIRIIRKASLYSSKAVLKED
APKEWDIRFLNTAVKISSSLKPDELLVLLKDIELKIGRDLNAPAWSPRVI
DLDILAAEDLILETDKLTIPHKELINRSFALAPLLELSKGWHHPKYVEWD
LNIRLKELGEIVKLKQTLANTIRMGIVNLSNQSFSDGNFDDNQRKLNLDE
LIQSGAEIIDIGAESTKPDAKPISIEEEFNKLDEFLEYFKSQLANLIYKP
LVSIDTRKLEVMQKILAKHHDIIWMINDVECNNIEQKAQLIAKYNKKYVI
IHNLGITDRNQYLDKENAIDNVCDYIEQKKQILLKHGIAQQNIYFDIGFG
FGKKSDTARYLLENIIEIKRRLELKALVGHSRKPSVLGLAKDSNLATLDR
ATRELSRKLEKLDIDIIRVHKI
3D structure
PDB8sl9 Crystal structure of Francisella tularensis HPPK-DHPS in complex with HPPK inhibitor HP-73
ChainA
Resolution1.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.15: dihydropteroate synthase.
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 H73 A K43 V45 F58 N60 L75 K79 R97 D100 D102 I103 K115 L116 T117 H120 R126 F128 K44 V46 F59 N61 L76 K80 R98 D101 D103 I104 K116 L117 T118 H121 R127 F129
Gene Ontology
Molecular Function
GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
GO:0004156 dihydropteroate synthase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0016310 phosphorylation
GO:0042558 pteridine-containing compound metabolic process
GO:0044237 cellular metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8sl9, PDBe:8sl9, PDBj:8sl9
PDBsum8sl9
PubMed
UniProtQ5NGA7

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