Structure of PDB 1a95 Chain B

Receptor sequence
>1a95B (length=150) Species: 562 (Escherichia coli) [Search protein sequence]
EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGI
RHVDTVCISSYDHDNQRELKVLKRAEGDGEGFIVIDDLVDTGGTAVAIRE
MYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPWDMGVVFVPPISGR
3D structure
PDB1a95 Structures of free and complexed forms of Escherichia coli xanthine-guanine phosphoribosyltransferase.
ChainB
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) D88 D89 D92
Catalytic site (residue number reindexed from 1) D86 D87 D90
Enzyme Commision number 2.4.2.-
2.4.2.22: xanthine 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 PCP B S36 R37 G38 R69 D88 D89 D92 T93 T96 S34 R35 G36 R67 D86 D87 D90 T91 T94
BS02 GUN B L90 D92 W134 I135 L88 D90 W132 I133
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0000310 xanthine phosphoribosyltransferase activity
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:0032263 GMP salvage
GO:0032264 IMP salvage
GO:0032265 XMP salvage
GO:0051289 protein homotetramerization
Cellular Component
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0032991 protein-containing complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:1a95, PDBe:1a95, PDBj:1a95
PDBsum1a95
PubMed9743633
UniProtP0A9M5|XGPT_ECOLI Xanthine-guanine phosphoribosyltransferase (Gene Name=gpt)

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