Structure of PDB 3fhx Chain A Binding Site BS02

Receptor Information
>3fhx Chain A (length=307) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHW
KGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELK
QQNPRLVYVCDPVLGDKWDGEGSMYVPEDLLPVYKEKVVPLADIITPNQF
EAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGSNYLIVL
GSQRRRNSVVMERIRMDIRKVDAVFVGTGALFAAMLLAWTHKHPNNLKVA
CEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDIEDPEI
VVQATVL
Ligand information
Ligand IDPXL
InChIInChI=1S/C8H9NO3/c1-5-8(12)7(4-11)6(3-10)2-9-5/h2,4,10,12H,3H2,1H3
InChIKeyRADKZDMFGJYCBB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)CO)C=O)O
ACDLabs 10.04O=Cc1c(cnc(c1O)C)CO
CACTVS 3.341Cc1ncc(CO)c(C=O)c1O
FormulaC8 H9 N O3
Name3-HYDROXY-5-(HYDROXYMETHYL)-2-METHYLISONICOTINALDEHYDE;
PYRIDOXAL
ChEMBLCHEMBL102970
DrugBankDB00147
ZINCZINC000000120249
PDB chain3fhx Chain A Residue 313 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3fhx Kinetic and structural studies of the role of the active site residue Asp235 of human pyridoxal kinase.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		S12 H46 T47 V231
Binding residue
(residue number reindexed from 1)		S10 H44 T45 V226
Annotation score5
Enzymatic activity
Enzyme Commision number 2.7.1.35: pyridoxal kinase.
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: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:0005576 extracellular region
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0034774 secretory granule lumen
GO:0035580 specific granule lumen
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3fhx, PDBe:3fhx, PDBj:3fhx
PDBsum3fhx
PubMed19351586
UniProtO00764|PDXK_HUMAN Pyridoxal kinase (Gene Name=PDXK)

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