Structure of PDB 3b1r Chain C

Receptor sequence
>3b1rC (length=310) Species: 271848 (Burkholderia thailandensis E264) [Search protein sequence]
ATLICGSIAYDNIMTFEGRFREHILPDQVHLINLSFLVPTMRREFGGCAG
NIAYALNLLGGDARMMGTLGAVDAQPYLDRMDALGLSREYVRVLPDTYSA
QAMITTDLDNNQITAFHPGAMMQSHVNHAGEAKDIKLAIVGPDGFQGMVQ
HTEELAQAGVPFIFDPGQGLPLFDGATLRRSIELATYIAVNDYEAKLVCD
KTGWSEDEIASRVQALIITRGEHGATIRHRDGTEQIPAVRAERVIDPTGC
GDAFRGGLLYGIEHGFDWATAGRLASLMGALKIAHQGPQTYAPTRAEIDA
RFETAFGYRP
3D structure
PDB3b1r Structures of Burkholderia thailandensis nucleoside kinase: implications for the catalytic mechanism and nucleoside selectivity
ChainC
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D247 P248 G250 C251
Catalytic site (residue number reindexed from 1) D246 P247 G249 C250
Enzyme Commision number 2.7.1.143: diphosphate-purine nucleoside 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 AMP C S8 D12 G48 C49 N52 Q113 F117 M122 Q169 G250 D253 S7 D11 G47 C48 N51 Q112 F116 M121 Q168 G249 D252
BS02 AMP C T220 G222 G225 C251 F255 S277 G280 I284 T219 G221 G224 C250 F254 S276 G279 I283
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016301 kinase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
Biological Process
GO:0016310 phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:3b1r, PDBe:3b1r, PDBj:3b1r
PDBsum3b1r
PubMed22101821
UniProtQ2SZE4

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