Structure of PDB 1eiy Chain A

Receptor sequence

>1eiyA (length=345) Species: 300852 (Thermus thermophilus HB8)

LAAIQNARDLEELKALKARYLGKKGLLTQEMKGLSALPLEERRKRGQELN
AIKAALEAALEAREKALEEAALKEALERERVDVSLPGASLFSGGLHPITL
MERELVEIFRALGYQAVEGPEVESEFFNFDALNIPEHHPARDMWDTFWLT
GEGFRLEGPLGEEVEGRLLLRTHTSPMQVRYMVAHTPPFRIVVPGRVFRF
EQTDATHEAVFHQLEGLVVGEGIAMAHLKGAIYELAQALFGPDSKVRFQP
VYFPFVEPGAQFAVWWPEGGKWLELGGAGMVHPKVFQAVDAYRERLGLPP
AYRGVTGFAFGLGVERLAMLRYGIPDIRYFFGGRLKFLEQFKGVL

3D structure

• PDB: 1eiy The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe.
• Chain: A
• Resolution: 3.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): W149 H178 R204 Q218 V261 A314
• Catalytic site (residue number reindexed from 1): W144 H173 R199 Q213 V256 A309
• 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	rna	A	M148 W149 E220 G316	M143 W144 E215 G311

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

External links

• PDB: RCSB:1eiy, PDBe:1eiy, PDBj:1eiy
• PDBsum: 1eiy
• PubMed: 9016717
• UniProt: Q5SGX2|SYFA_THET8 Phenylalanine--tRNA ligase alpha subunit (Gene Name=pheS)