Structure of PDB 1b7y Chain A

Receptor sequence
>1b7yA (length=265) Species: 274 (Thermus thermophilus) [Search protein sequence]
VDVSLPGASLFSGGLHPITLMERELVEIFRALGYQAVEGPEVESEFFNFD
ALNIPEHHPARDMWDTFWLTGEGFRLEGPLGEEVEGRLLLRTHTSPMQVR
YMVAHTPPFRIVVPGRVFRFEQTDATHEAVFHQLEGLVVGEGIAMAHLKG
AIYELAQALFGPDSKVRFQPVYFPFVEPGAQFAVWWPEGGKWLELGGAGM
VHPKVFQAVDAYRERLGLPPAYRGVTGFAFGLGVERLAMLRYGIPDIRYF
FGGRLKFLEQFKGVL
3D structure
PDB1b7y Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W149 H178 R204 Q218 V261 A314
Catalytic site (residue number reindexed from 1) W64 H93 R119 Q133 V176 A229
Enzyme Commision number 6.1.1.20: phenylalanine--tRNA ligase.
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 FYA A R204 E206 E213 F216 Q218 E220 F258 L280 G282 A283 A314 F315 G316 G318 R321 R119 E121 E128 F131 Q133 E135 F173 L195 G197 A198 A229 F230 G231 G233 R236
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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Cellular Component
External links
PDB RCSB:1b7y, PDBe:1b7y, PDBj:1b7y
PDBsum1b7y
PubMed10092459
UniProtP27001|SYFA_THETH Phenylalanine--tRNA ligase alpha subunit (Gene Name=pheS)

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