Structure of PDB 5vjn Chain A

Receptor sequence
>5vjnA (length=176) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
IASYAQELKLALHQYPNFPSEGILFEDFLPIFRNPGLFQKLIDAFKLHLE
EAFPEVKIDYIVGLESRGFLFGPTLALALGVGFVPVRKAGKLPGECFKAT
YEKEYGSDLFEIQKNAIPAGSNVIIVDDIIATGGSAAAAGELVEQLEANL
LEYNFVMELDFLKGRSKLNAPVFTLL
3D structure
PDB5vjn Synthesis of bis-Phosphate Iminoaltritol Enantiomers and Structural Characterization with Adenine Phosphoribosyltransferase.
ChainA
Resolution1.78 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R69
Catalytic site (residue number reindexed from 1) R67
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 IR8 A R69 D129 D130 A133 T134 G135 S137 R67 D127 D128 A131 T132 G133 S135 MOAD: Ki=8.7uM
PDBbind-CN: -logKd/Ki=5.06,Ki=8.7uM
BS02 ADE A L26 F27 I131 A133 L161 L24 F25 I129 A131 L159
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
GO:0046872 metal ion binding
Biological Process
GO:0006166 purine ribonucleoside salvage
GO:0006168 adenine salvage
GO:0009058 biosynthetic process
GO:0044209 AMP salvage
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5vjn, PDBe:5vjn, PDBj:5vjn
PDBsum5vjn
PubMed29178779
UniProtP49435|APT1_YEAST Adenine phosphoribosyltransferase 1 (Gene Name=APT1)

[Back to BioLiP]