Structure of PDB 1kzh Chain B

Receptor sequence
>1kzhB (length=530) Species: 139 (Borreliella burgdorferi) [Search protein sequence]
TSLFKQERQKYIPKLPNILKKDFNNISLVYGENTEAIQDRQALKEFFKNT
YGLPIISFTEGESSLSFSKALNIGIILSGGPAPGGHNVISGVFDAIKKFN
PNSKLFGFKGGPLGLLENDKIELTESLINSYRNTGGFDIVSSGRTKIETE
EHYNKALFVAKENNLNAIIIIGGDDSNTNAAILAEYFKKNGENIQVIGVP
KTIDADLRNDHIEISFGFDSATKIYSELIGNLCRDAMSTKKYWHFVKLMG
RSASHVALECALKTHPNICIVSEEVLAKKKTLSEIIDEMVSVILKRSLNG
DNFGVVIVPEGLIEFIPEVKSLMLELCDIFIEKMKEIFVAKLSDYMKGVY
LSLPLFIQFELIKSILERVPTEKLFIEMIQSRLNDMKKRGEYKGSFTPVD
HFFGYEGRSAFPSNFDSDYCYSLGYNAVVLILNGLTGYMSCIKNLNLKPT
DWIAGGVPLTMLMNMEERYGEKKPVIKKALVDLEGRPFKEFVKNRDKWAL
NNLYLYPGPVQYFGSSEIVDEITETLKLEL
3D structure
PDB1kzh The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi.
ChainB
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G82 G145 R146 D176 D177 K203 T204 D206 D208 R253
Catalytic site (residue number reindexed from 1) G80 G143 R144 D174 D175 K201 T202 D204 D206 R251
Enzyme Commision number 2.7.1.90: diphosphate--fructose-6-phosphate 1-phosphotransferase.
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 SO4 B T241 K243 Y244 T239 K241 Y242
BS02 SO4 B R146 R431 R144 R408
BS03 SO4 B S80 G81 G175 D177 S178 S78 G79 G173 D175 S176
BS04 SO4 B K71 N102 K69 N100
BS05 SO4 B K23 D24 N27 K21 D22 N25
Gene Ontology
Molecular Function
GO:0003872 6-phosphofructokinase activity
GO:0005524 ATP binding
GO:0008443 phosphofructokinase activity
GO:0016301 kinase activity
GO:0046872 metal ion binding
GO:0047334 diphosphate-fructose-6-phosphate 1-phosphotransferase activity
Biological Process
GO:0006002 fructose 6-phosphate metabolic process
GO:0006096 glycolytic process
GO:0009749 response to glucose
GO:0016310 phosphorylation
GO:0046835 carbohydrate phosphorylation
GO:0061615 glycolytic process through fructose-6-phosphate
Cellular Component
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:1kzh, PDBe:1kzh, PDBj:1kzh
PDBsum1kzh
PubMed12015149
UniProtP70826|PFP_BORBU Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (Gene Name=pfp)

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