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Structure of PDB 1rxc Chain J Binding Site BS03

Receptor Information >1rxc Chain J (length=250) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] SDVFHLGLTKNDLQGATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTW RAELDGKPVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHIN VGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHV GVTASSDTFYPGQERYDTYSGRVVRHFKGSMEEWQAMGVMNYEMESATLL TMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVVEAARRLL

Ligand information Ligand ID PO4 InChI InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3 InChIKey NBIIXXVUZAFLBC-UHFFFAOYSA-K SMILES Software SMILES CACTVS 3.341 [O-][P]([O-])([O-])=O ACDLabs 10.04 [O-]P([O-])([O-])=O OpenEye OEToolkits 1.5.0 [O-]P(=O)([O-])[O-] Formula O4 P Name PHOSPHATE ION ChEMBL DrugBank DB14523 ZINC PDB chain 1rxc Chain J Residue 2052 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 1rxc Crystal structures of escherichia coli uridine phosphorylase in two native and three complexed forms reveal basis of substrate specificity, induced conformational changes and influence of potassium Resolution 2.35 Å Binding residue (original residue number in PDB) G26 R30 R91 G93 T94 Binding residue (residue number reindexed from 1) G23 R27 R88 G90 T91 Annotation score 1

Enzymatic activity Catalytic site (original residue number in PDB) H8 G26 R30 R48 E80 R91 T94 R168 I220 V221 R223 M234 Catalytic site (residue number reindexed from 1) H5 G23 R27 R45 E77 R88 T91 R165 I217 V218 R220 M231 Enzyme Commision number 2.4.2.3: uridine phosphorylase.

Gene Ontology Molecular Function GO:0003824 catalytic activity GO:0004850 uridine phosphorylase activity GO:0005524 ATP binding GO:0016757 glycosyltransferase activity GO:0016763 pentosyltransferase activity GO:0030955 potassium ion binding GO:0042802 identical protein binding GO:0047847 deoxyuridine phosphorylase activity

	Biological Process
GO:0006218	uridine catabolic process
GO:0006974	DNA damage response
GO:0009116	nucleoside metabolic process
GO:0009164	nucleoside catabolic process
GO:0009166	nucleotide catabolic process
GO:0044206	UMP salvage
GO:0046050	UMP catabolic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0032991	protein-containing complex

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