Structure of PDB 4i5v Chain B

Receptor sequence
>4i5vB (length=295) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MIEENLKQKIHDKFVAAKKNGHLKVTHAESKKLKDPQTTTQYWVTFAPSL
ALKPDPFANPDEELVVTEDLNGDGEYKLLLNKFPVVPEHSLLVTSEFKDQ
RSALTPSDLMTAYNVLCSLQGDKDDDVTCERYLVFYNCGPHSGSSQDHKA
LQIMQMPEKFIPFQDVLCNGKDHFLPTFNAEPLQDDKVSFAHFVLPLPES
SDQVDEDLLAMCYVSLMQRALTFFTKSYNVLLTKKWICVVPRSHAKSGPP
LMLNINSTGYCGMILVKDREKLENLTEDPHLVDKSLLQCGFPNTA
3D structure
PDB4i5v Structures of yeast Apa2 reveal catalytic insights into a canonical AP4A phosphorylase of the histidine triad superfamily
ChainB
Resolution2.696 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.5: sulfate adenylyltransferase (ADP).
2.7.7.53: ATP adenylyltransferase.
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 B4P B P67 N92 K93 F94 V96 N148 G154 S155 S156 Q157 Q163 M165 N277 T279 M284 P56 N81 K82 F83 V85 N137 G143 S144 S145 Q146 Q152 M154 N256 T258 M263
Gene Ontology
Molecular Function
GO:0003877 ATP:ADP adenylyltransferase activity
GO:0004780 sulfate adenylyltransferase (ADP) activity
GO:0005524 ATP binding
GO:0008796 bis(5'-nucleosyl)-tetraphosphatase activity
GO:0016779 nucleotidyltransferase activity
GO:0016787 hydrolase activity
GO:0033699 DNA 5'-adenosine monophosphate hydrolase activity
Biological Process
GO:0009117 nucleotide metabolic process
GO:0009164 nucleoside catabolic process
GO:0009165 nucleotide biosynthetic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:4i5v, PDBe:4i5v, PDBj:4i5v
PDBsum4i5v
PubMed23628156
UniProtP22108|APA2_YEAST Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase 2 (Gene Name=APA2)

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