Structure of PDB 2i5b Chain A

Receptor sequence
>2i5bA (length=269) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVIVAMDPNNSWNH
QVFPIDTDTIRAQLATITDGIGVDAMKTGMLPTVDIIELAAKTIKEKQLK
NVVIDPVMVCKGANEVLYPEHAQALREQLAPLATVITPNLFEASQLSGMD
ELKTVDDMIEAAKKIHALGAQYVVITGGGKLKHEKAVDVLYDGETAEVLE
SEMIDTPYTHGAGCTFSAAVTAELAKGAEVKEAIYAAKEFITAAIKESFP
LNQYVGPTKHSALRLNQQS
3D structure
PDB2i5b The Crystal Structure of an ADP Complex of Bacillus subtilis Pyridoxal Kinase Provides Evidence for the Parallel Emergence of Enzyme Activity During Evolution.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T178 T211 G213 A214 G215 C216
Catalytic site (residue number reindexed from 1) T176 T209 G211 A212 G213 C214
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 ADP A N141 T178 G180 G181 K182 A188 D190 I206 A214 G215 I247 N139 T176 G178 G179 K180 A186 D188 I204 A212 G213 I245
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008478 pyridoxal kinase activity
GO:0008902 hydroxymethylpyrimidine kinase activity
GO:0008972 phosphomethylpyrimidine kinase activity
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0009228 thiamine biosynthetic process
GO:0016310 phosphorylation
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2i5b, PDBe:2i5b, PDBj:2i5b
PDBsum2i5b
PubMed16978644
UniProtP39610|PDXK_BACSU Pyridoxine kinase (Gene Name=pdxK)

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