Structure of PDB 6hgq Chain D

Receptor sequence

>6hgqD (length=177) Species: 9606 (Homo sapiens)

SELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKAT
HGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSL
EYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLEC
VSLVELTSLKGREKLAPVPFFSLLQYE

3D structure

• PDB: 6hgq Structural basis for substrate selectivity and nucleophilic substitution mechanisms in human adenine phosphoribosyltransferase catalyzed reaction.
• Chain: D
• Resolution: 1.9 Å

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	D	R87 K91	R84 K88
BS02	PRP	D	S66 R67 K88 L103 Y105 D127 D128 L129 A131 T132 G133 T135	S63 R64 K85 L100 Y102 D124 D125 L126 A128 T129 G130 T132
BS03	HPA	D	F26 R27 R67 E104 Y105 L129	F23 R24 R64 E101 Y102 L126

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

External links

• PDB: RCSB:6hgq, PDBe:6hgq, PDBj:6hgq
• PDBsum: 6hgq
• PubMed: 31160323
• UniProt: P07741|APT_HUMAN Adenine phosphoribosyltransferase (Gene Name=APRT)