Structure of PDB 2nqp Chain C

Receptor sequence
>2nqpC (length=264) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
PPVYKIALGIEYDGSKYYGWQRQNEVRSVQEKLEKALSQVANEPITVFCA
GRTDAGVHGTGQVVHFETTALRKDAAWTLGVNANLPGDIAVRWVKTVPDD
FHARFSATARRYRYIIYNHRLRPAVLSKGVTHFYEPLDAERMHRAAQCLL
GENDFTSFRAVQCQSRTPWRNVMHINVTRHGPYVVVDIKANAFVHHMVRN
IVGSLMEVGAHNQPESWIAELLAAKDRTLAAATAKAEGLYLVAVDYPDRY
DLPKPPMGPLFLAD
3D structure
PDB2nqp How U38, 39, and 40 of Many tRNAs Become the Targets for Pseudouridylation by TruA.
ChainC
Resolution3.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R58 D60 R205
Catalytic site (residue number reindexed from 1) R52 D54 R199
Enzyme Commision number 5.4.99.12: tRNA pseudouridine(38-40) synthase.
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 rna C Q45 V46 N48 R78 A81 A82 L85 A89 N90 Q39 V40 N42 R72 A75 A76 L79 A83 N84
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:2nqp, PDBe:2nqp, PDBj:2nqp
PDBsum2nqp
PubMed17466622
UniProtP07649|TRUA_ECOLI tRNA pseudouridine synthase A (Gene Name=truA)

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