Structure of PDB 1ore Chain A

Receptor sequence
>1oreA (length=179) Species: 9606 (Homo sapiens) [Search protein sequence]
ADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLK
ATHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASY
SLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVL
ECVSLVELTSLKGREKLAPVPFFSLLQYE
3D structure
PDB1ore Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R67 E104
Catalytic site (residue number reindexed from 1) R66 E103
Enzyme Commision number 2.4.2.7: adenine 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 AMP A F26 R27 R67 D127 D128 L129 A131 T132 G133 T135 F25 R26 R66 D126 D127 L128 A130 T131 G132 T134
Gene Ontology
Molecular Function
GO:0002055 adenine binding
GO:0003999 adenine phosphoribosyltransferase activity
GO:0005515 protein binding
GO:0016208 AMP binding
GO:0016757 glycosyltransferase activity
Biological Process
GO:0006166 purine ribonucleoside salvage
GO:0006168 adenine salvage
GO:0007625 grooming behavior
GO:0032263 GMP salvage
GO:0032264 IMP salvage
GO:0044209 AMP salvage
GO:0046083 adenine metabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0034774 secretory granule lumen
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ore, PDBe:1ore, PDBj:1ore
PDBsum1ore
PubMed15196008
UniProtP07741|APT_HUMAN Adenine phosphoribosyltransferase (Gene Name=APRT)

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