Structure of PDB 5knx Chain B

Receptor sequence
>5knxB (length=176) Species: 562 (Escherichia coli) [Search protein sequence]
DMKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFM
ADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLIVE
DIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIP
DEFVVGYGIDYAQRYRHLPYIGKVIL
3D structure
PDB5knx Crystal Structures of Acyclic Nucleoside Phosphonates in Complex with Escherichia coli Hypoxanthine Phosphoribosyltransferase
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E103 D104 D107 F156 R169
Catalytic site (residue number reindexed from 1) E100 D101 D104 F153 R166
Enzyme Commision number 2.4.2.8: hypoxanthine phosphoribosyltransferase.
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 6WC B S73 D107 S108 G109 K135 F156 V157 I162 S70 D104 S105 G106 K132 F153 V154 I159 PDBbind-CN: -logKd/Ki=6.10,Ki=0.8uM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004422 hypoxanthine phosphoribosyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0052657 guanine phosphoribosyltransferase activity
GO:0097216 guanosine tetraphosphate binding
Biological Process
GO:0006166 purine ribonucleoside salvage
GO:0006178 guanine salvage
GO:0032263 GMP salvage
GO:0032264 IMP salvage
GO:0046100 hypoxanthine metabolic process
GO:0051289 protein homotetramerization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:5knx, PDBe:5knx, PDBj:5knx
PDBsum5knx
PubMed
UniProtP0A9M2|HPRT_ECOLI Hypoxanthine phosphoribosyltransferase (Gene Name=hpt)

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