Structure of PDB 3fhx Chain B

Receptor sequence
>3fhxB (length=310) Species: 9606 (Homo sapiens) [Search protein sequence]
EECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHW
KGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELK
QQNPRLVYVCDPVLGDKWDGEGSMYVPEDLLPVYKEKVVPLADIITPNQF
EAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGSNYLIVL
GSQRRRNPAGSVVMERIRMDIRKVDAVFVGTGALFAAMLLAWTHKHPNNL
KVACEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDIED
PEIVVQATVL
3D structure
PDB3fhx Kinetic and structural studies of the role of the active site residue Asp235 of human pyridoxal kinase.
ChainB
Resolution2.5 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 ATP B D113 N150 E153 T186 S187 L199 K225 V226 T233 L267 D111 N148 E151 T184 S185 L197 K223 V224 T231 L265
BS02 PXL B S12 F43 H46 T47 S10 F41 H44 T45
BS03 PLP B V231 G232 V229 G230
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

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

[Back to BioLiP]