Structure of PDB 2iy5 Chain A

Receptor sequence
>2iy5A (length=336) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
LEELKALKARYLGKKGLLTQEMKGLSALPLEERRKRGQELNAIKAALEAA
LEAREKALEEAALKEALERERVDVSLPGASLFSGGLHPITLMERELVEIF
RALGYQAVEGPEVESEFFNFDALNIPEHHPARDMWDTFWLTGEGFRLEGP
LGEEVEGRLLLRTHTSPMQVRYMVAHTPPFRIVVPGRVFRFEQTDATHEA
VFHQLEGLVVGEGIAMAHLKGAIYELAQALFGPDSKVRFQPVYFPFVEPG
AQFAVWWPEGGKWLELGGAGMVHPKVFQAVDAYRERLGLPPAYRGVTGFA
FGLGVERLAMLRYGIPDIRYFFGGRLKFLEQFKGVL
3D structure
PDB2iy5 The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end.
ChainA
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W149 H178 R204 Q218 V261 A314
Catalytic site (residue number reindexed from 1) W135 H164 R190 Q204 V247 A300
Enzyme Commision number 6.1.1.20: phenylalanine--tRNA ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004826 phenylalanine-tRNA ligase activity
GO:0005524 ATP binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006432 phenylalanyl-tRNA aminoacylation
GO:0043039 tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2iy5, PDBe:2iy5, PDBj:2iy5
PDBsum2iy5
PubMed16939209
UniProtQ5SGX2|SYFA_THET8 Phenylalanine--tRNA ligase alpha subunit (Gene Name=pheS)

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