Structure of PDB 6yk0 Chain C

Receptor sequence
>6yk0C (length=309) Species: 10090 (Mus musculus) [Search protein sequence]
ECRVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWK
GQVLKSQELHELYEGLKVNDVNKYDYVLTGYTRDKSFLAMVVDIVRELKQ
QNSRLVYVCDPVMGDKWNGEGSMYVPQDLLPVYRDKVVPVADIITPNQFE
AELLSGRKIHSQEEAFEVMDMLHCMGPDTVVITSSDLPSSQGSDYLIALG
SQRMRKPDGSTVTQRIRMEMRKVEAVFVGTGDLFAAMLLAWTHKHPDNLK
VACEKTVSAMQHVLQRTIRCAKAEAGEGQKPSPAQLELRMVQSKRDIEDP
EIVVQATVL
3D structure
PDB6yk0 Pyridoxal kinase inhibition by artemisinins down-regulates inhibitory neurotransmission.
ChainC
Resolution2.9 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 AGS C D113 D118 N150 E153 T186 S187 M223 V226 T233 L267 D110 D115 N147 E150 T183 S184 M220 V223 T230 L264
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0008478 pyridoxal kinase activity
GO:0016301 kinase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
GO:0030170 pyridoxal phosphate binding
GO:0030955 potassium ion binding
GO:0031402 sodium ion binding
GO:0031403 lithium ion binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0008614 pyridoxine metabolic process
GO:0009443 pyridoxal 5'-phosphate salvage
GO:0016310 phosphorylation
GO:0042816 vitamin B6 metabolic process
GO:0042817 pyridoxal metabolic process
GO:0042818 pyridoxamine metabolic process
GO:0042822 pyridoxal phosphate metabolic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
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:6yk0, PDBe:6yk0, PDBj:6yk0
PDBsum6yk0
PubMed33318193
UniProtQ8K183|PDXK_MOUSE Pyridoxal kinase (Gene Name=Pdxk)

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