Structure of PDB 6su9 Chain A Binding Site BS03
Receptor Information
>6su9 Chain A (length=295) Species:
36329
(Plasmodium falciparum 3D7) [
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MKKENIISIQSQVFDGFCGNNIAAFVFRRRGHIPKILNTVQYYSKFKHSG
VELNSQEVDIILSEYNKDQENDSNIYFLTGYIKNAECVDMVTKNILELRR
KRKIHYFIENIINLNFLWVCDPVMGDNGRLYVDERVVESYKKAIEYVDII
TPNQYETELLCGIKINEEKDVIKCLDVLLHKGVKIVIITSVNYNFDKDHL
FLYVSFFNNKNKIVYFKYKILKIHFNCFGSGDLFSCLLLSFIVKQKGNIL
HIISKVLNIVQNVIKNSLTGLELNIIENQDIIASDDILIKEEPVF
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
6su9 Chain A Residue 704 [
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Receptor-Ligand Complex Structure
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PDB
6su9
Crystal structure of Plasmodium falciparum PdxK with ligands AMP-PNP and PL.
Resolution
2.15 Å
Binding residue
(original residue number in PDB)
F25 R28
Binding residue
(residue number reindexed from 1)
F25 R28
Annotation score
1
Enzymatic activity
Enzyme Commision number
2.7.1.35
: pyridoxal kinase.
Gene Ontology
Molecular Function
GO:0005524
ATP binding
GO:0008478
pyridoxal kinase activity
GO:0016301
kinase activity
GO:0046872
metal ion binding
GO:0070280
pyridoxal binding
GO:0070281
pyridoxamine binding
GO:0070282
pyridoxine binding
Biological Process
GO:0000304
response to singlet oxygen
GO:0008614
pyridoxine metabolic process
GO:0009443
pyridoxal 5'-phosphate salvage
GO:0016310
phosphorylation
GO:0042816
vitamin B6 metabolic process
GO:0042819
vitamin B6 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:6su9
,
PDBe:6su9
,
PDBj:6su9
PDBsum
6su9
PubMed
UniProt
C6KT01
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