Structure of PDB 5vjp Chain B

Receptor sequence
>5vjpB (length=179) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MPIASYAQELKLALHQYPNFPSEGILFEDFLPIFRNPGLFQKLIDAFKLH
LEEAFPEVKIDYIVGLESRGFLFGPTLALALGVGFVPVRKAGKLPGECFK
ATYEKEYGSDLFEIQKNAIPAGSNVIIVDDIIATGGSAAAAGELVEQLEA
NLLEYNFVMELDFLKGRSKLNAPVFTLLN
3D structure
PDB5vjp Synthesis of bis-Phosphate Iminoaltritol Enantiomers and Structural Characterization with Adenine Phosphoribosyltransferase.
ChainB
Resolution1.98 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R69 E106
Catalytic site (residue number reindexed from 1) R69 E106
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 IR9 B D129 D130 I131 A133 T134 G135 G136 S137 D129 D130 I131 A133 T134 G135 G136 S137 MOAD: Ki=14.9uM
PDBbind-CN: -logKd/Ki=4.83,Ki=14.9uM
BS02 ADE B L26 E28 R69 I131 L161 L26 E28 R69 I131 L161
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:5vjp, PDBe:5vjp, PDBj:5vjp
PDBsum5vjp
PubMed29178779
UniProtP49435|APT1_YEAST Adenine phosphoribosyltransferase 1 (Gene Name=APT1)

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