Structure of PDB 4tva Chain A

Receptor sequence
>4tvaA (length=266) Species: 274 (Thermus thermophilus) [Search protein sequence]
RVDVSLPGASLFSGGLHPITLMERELVEIFRALGYQAVEGPEVESEFFNF
DALNIPEHHPARDMWDTFWLTGEGFRLEGPLGEEVEGRLLLRTHTSPMQV
RYMVAHTPPFRIVVPGRVFRFEQTDATHEAVFHQLEGLVVGEGIAMAHLK
GAIYELAQALFGPDSKVRFQPVYFPFVEPGAQFAVWWPEGGKWLELGGAG
MVHPKVFQAVDAYRERLGLPPAYRGVTGFAFGLGVERLAMLRYGIPDIRY
FFGGRLKFLEQFKGVL
3D structure
PDB4tva Universal pathway for posttransfer editing reactions: Insights from the crystal structure of TtPheRS with puromycin.
ChainA
Resolution2.597 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) W65 H94 R120 Q134 V177 A230
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 PHE A H178 E220 F258 F260 G282 A283 A314 F315 G316 H94 E136 F174 F176 G198 A199 A230 F231 G232
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:4tva, PDBe:4tva, PDBj:4tva
PDBsum4tva
PubMed25775602
UniProtP27001|SYFA_THETH Phenylalanine--tRNA ligase alpha subunit (Gene Name=pheS)

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