Structure of PDB 5kns Chain B

Receptor sequence
>5knsB (length=172) Species: 562 (Escherichia coli) [Search protein sequence]
DMKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFM
ADLCREVQVSHEVDFMTASSTTRDVKILKDLDEDIRGKDVLIVEDIIDSG
NTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVG
YGIDYAQRYRHLPYIGKVILLD
3D structure
PDB5kns Crystal Structures of Acyclic Nucleoside Phosphonates in Complex with Escherichia coli Hypoxanthine Phosphoribosyltransferase
ChainB
Resolution2.792 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) E94 D95 D98 F147 R160
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 3L7 B D107 S108 G109 T111 K135 F156 V157 D163 R169 D98 S99 G100 T102 K126 F147 V148 D154 R160 PDBbind-CN: -logKd/Ki=6.12,Ki=0.75uM
BS02 MG B E103 D104 E94 D95
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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Biological Process
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Cellular Component
External links
PDB RCSB:5kns, PDBe:5kns, PDBj:5kns
PDBsum5kns
PubMed
UniProtP0A9M2|HPRT_ECOLI Hypoxanthine phosphoribosyltransferase (Gene Name=hpt)

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