Structure of PDB 4i5w Chain B

Receptor sequence
>4i5wB (length=282) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
MIEENLKQKIHDKFVAAKKNGHLKVTHAESKKLKDPQTTTQYWVTFAPSL
DPFANPDEELVVTEDLNGDGEYKLLLNKFPVVPEHSLLVTSEFKDQRSAL
TPSDLMTAYNVLCSLQGTCERYLVFYNCGPHSGSSQDHKHLQIMQMPEKF
IPFQDVLCNGKDHAEPLQDDKVSFAHFVLPLPESSDQVDEDLLAMCYVSL
MQRALTFFQELTKSYNVLLTKKWICVVPRSHAKSGPPLMLNINSTGYCGM
ILVKDREKLENLTEDPHLVDKSLLQCGFPNTA
3D structure
PDB4i5w Structures of yeast Apa2 reveal catalytic insights into a canonical AP4A phosphorylase of the histidine triad superfamily
ChainB
Resolution2.793 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 AMP B L75 N92 K93 F94 L102 S155 S156 H161 L60 N77 K78 F79 L87 S134 S135 H140
BS02 AMP B N92 F94 V96 V97 H100 M165 T279 N77 F79 V81 V82 H85 M144 T245
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:4i5w, PDBe:4i5w, PDBj:4i5w
PDBsum4i5w
PubMed23628156
UniProtP22108|APA2_YEAST Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase 2 (Gene Name=APA2)

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