Structure of PDB 6fci Chain B

Receptor sequence
>6fciB (length=177) Species: 9606 (Homo sapiens) [Search protein sequence]
SELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKAT
HGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSL
EYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLEC
VSLVELTSLKGREKLAPVPFFSLLQYE
3D structure
PDB6fci Structural Insights into the Forward and Reverse Enzymatic Reactions in Human Adenine Phosphoribosyltransferase.
ChainB
Resolution1.94 Å
3D
structure
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Enzymatic activity
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 PRP B S66 R67 K88 L103 Y105 D127 D128 L129 A131 T132 G133 T135 S63 R64 K85 L100 Y102 D124 D125 L126 A128 T129 G130 T132
BS02 ADE B F26 R27 R67 E104 Y105 L129 F23 R24 R64 E101 Y102 L126
BS03 PRP B R87 K91 R84 K88
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:6fci, PDBe:6fci, PDBj:6fci
PDBsum6fci
PubMed29576532
UniProtP07741|APT_HUMAN Adenine phosphoribosyltransferase (Gene Name=APRT)

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