Structure of PDB 3teh Chain A

Receptor sequence

>3tehA (length=266) Species: 274 (Thermus thermophilus)

RVDVSLPGASLFSGGLHPITLMERELVEIFRALGYQAVEGPEVESEFFNF
DALNIPEHHPARDMWDTFWLTGEGFRLEGPLGEEVEGRLLLRTHTSPMQV
RYMVAHTPPFRIVVPGRVFRFEQTDATHEAVFHQLEGLVVGEGIAMAHLK
GAIYELAQALFGPDSKVRFQPVYFPFVEPGAQFAVWWPEGGKWLELGGAG
MVHPKVFQAVDAYRERLGLPPAYRGVTGFAFGLGVERLAMLRYGIPDIRY
FFGGRLKFLEQFKGVL

3D structure

• PDB: 3teh Bacterial and Eukaryotic Phenylalanyl-tRNA Synthetases Catalyze Misaminoacylation of tRNA(Phe) with 3,4-Dihydroxy-L-Phenylalanine.
• Chain: A
• Resolution: 2.8524 Å

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	DAH	A	H178 Q218 E220 F260 G282 A283 A314 F315 G316	H94 Q134 E136 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

External links

• PDB: RCSB:3teh, PDBe:3teh, PDBj:3teh
• PDBsum: 3teh
• PubMed: 22035791
• UniProt: P27001|SYFA_THETH Phenylalanine--tRNA ligase alpha subunit (Gene Name=pheS)