Structure of PDB 2ia5 Chain J

Receptor sequence
>2ia5J (length=296) Species: 10665 (Tequatrovirus T4) [Search protein sequence]
MKKIILTIGCPGSGKSTWAREFIAKNPGFYNINRDDYRQSIMAHEERDEY
KYTKKKEGIVTGMQFDTAKSILYGGDSVKGVIISDTNLNPERRLAWETFA
KEYGWKVEHKVFDVPWTELVKRNSKRGTKAVPIDVLRSMYKSMREYLGLP
VYNGTPGKPKAVIFDVDGTLAKMNPYDLCDTDVINPMVVELSKMYALMGY
QIVVVSGRESGTKEDPTKYYRMTRKWVEDIAGVPLVMQCQREQGDTRKDD
VVKEEIFWKHIAPHFDVKLAIDDRTQVVEMWRRIGVECWQVASGDF
3D structure
PDB2ia5 Structure-function analysis of the 3' phosphatase component of T4 polynucleotide kinase/phosphatase.
ChainJ
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K15 D35 R126 D165
Catalytic site (residue number reindexed from 1) K15 D35 R126 D165
Enzyme Commision number 2.7.1.78: polynucleotide 5'-hydroxyl-kinase.
3.1.3.34: deoxynucleotide 3'-phosphatase.
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 MG J D167 G168 T169 D278 D167 G168 T169 D273
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016787 hydrolase activity
GO:0046404 ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity
GO:0047846 deoxynucleotide 3'-phosphatase activity
GO:0051734 ATP-dependent polynucleotide 5'-hydroxyl-kinase activity
Biological Process
GO:0006281 DNA repair
GO:0016310 phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2ia5, PDBe:2ia5, PDBj:2ia5
PDBsum2ia5
PubMed17493655
UniProtP06855|KIPN_BPT4 Polynucleotide kinase (Gene Name=pseT)

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