Structure of PDB 6su9 Chain A

Receptor sequence
>6su9A (length=295) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
MKKENIISIQSQVFDGFCGNNIAAFVFRRRGHIPKILNTVQYYSKFKHSG
VELNSQEVDIILSEYNKDQENDSNIYFLTGYIKNAECVDMVTKNILELRR
KRKIHYFIENIINLNFLWVCDPVMGDNGRLYVDERVVESYKKAIEYVDII
TPNQYETELLCGIKINEEKDVIKCLDVLLHKGVKIVIITSVNYNFDKDHL
FLYVSFFNNKNKIVYFKYKILKIHFNCFGSGDLFSCLLLSFIVKQKGNIL
HIISKVLNIVQNVIKNSLTGLELNIIENQDIIASDDILIKEEPVF
3D structure
PDB6su9 Crystal structure of Plasmodium falciparum PdxK with ligands AMP-PNP and PL.
ChainA
Resolution2.15 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.1.35: pyridoxal kinase.
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 ANP A D323 N350 T386 S387 L397 I417 I420 F422 F425 G426 S427 G428 Q458 D126 N153 T189 S190 L200 I220 I223 F225 F228 G229 S230 G231 Q261
BS02 PXL A S11 C18 H48 D429 S11 C18 H48 D232
BS03 MG A F25 R28 F25 R28
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
PDBsum6su9
PubMed
UniProtC6KT01

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