Structure of PDB 2nr0 Chain D Binding Site BS01

Receptor Information
>2nr0 Chain D (length=264) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PPVYKIALGIEYDGSKYYGWQRQNEVRSVQEKLEKALSQVANEPITVFCA
GRTDAGVHGTGQVVHFETTALRKDAAWTLGVNANLPGDIAVRWVKTVPDD
FHARFSATARRYRYIIYNHRLRPAVLSKGVTHFYEPLDAERMHRAAQCLL
GENDFTSFRAVQCQSRTPWRNVMHINVTRHGPYVVVDIKANAFVHHMVRN
IVGSLMEVGAHNQPESWIAELLAAKDRTLAAATAKAEGLYLVAVDYPDRY
DLPKPPMGPLFLAD
Ligand information
>2nr0 Chain G (length=67) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
aggugguggaauugguagacacgcuaccuugaggugguagugcgcuuacg
gguucaagucccguccu
Receptor-Ligand Complex Structure
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PDB2nr0 How U38, 39, and 40 of Many tRNAs Become the Targets for Pseudouridylation by TruA.
Resolution3.9 Å
Binding residue
(original residue number in PDB)		V46 N48 R78 A82 L85 G86 N90
Binding residue
(residue number reindexed from 1)		V40 N42 R72 A76 L79 G80 N84
Binding affinityPDBbind-CN: Kd=1.05uM
Enzymatic activity
Enzyme Commision number 5.4.99.12: tRNA pseudouridine(38-40) synthase.
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0003723 RNA binding
GO:0009982 pseudouridine synthase activity
GO:0016853 isomerase activity
GO:0042803 protein homodimerization activity
GO:0106029 tRNA pseudouridine synthase activity
GO:0140098 catalytic activity, acting on RNA
GO:0160147 tRNA pseudouridine(38-40) synthase activity
Biological Process
GO:0001522 pseudouridine synthesis
GO:0006396 RNA processing
GO:0008033 tRNA processing
GO:0009451 RNA modification
GO:0031119 tRNA pseudouridine synthesis

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Molecular Function
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Biological Process
External links
PDB RCSB:2nr0, PDBe:2nr0, PDBj:2nr0
PDBsum2nr0
PubMed17466622
UniProtP07649|TRUA_ECOLI tRNA pseudouridine synthase A (Gene Name=truA)

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