Structure of PDB 2rhs Chain C

Receptor sequence

>2rhsC (length=271) Species: 1283 (Staphylococcus haemolyticus)

ELMEKLNQQLAEETIDVTLPSRQISIGSKHPLTRTVEEIEDLFLGLGYEI
VDGYEVEQDYYNFEALNLPKSHPARDMQDSFYITDEILMRTHTSPVQART
MEKRNGQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMSDLK
GTLELVAKKLFGADREIRLRPSYFPFTEPSVEVDVSCFKCKGKGCNVCKH
TGWIEILGAGMVHPNVLEMAGFDSNEYSGFAFGMGPDRIAMLKYGIEDIR
YFYTNDVRFLEQFKAVEDRGE

3D structure

• PDB: 2rhs Rational protein engineering in action: the first crystal structure of a phenylalanine tRNA synthetase from Staphylococcus haemolyticus.
• Chain: C
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q158 H172 R200 Q214 T257 A311
• Catalytic site (residue number reindexed from 1): Q78 H92 R120 Q134 T177 A231
• 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	ZN	C	C267 C270 C275 C278	C187 C190 C195 C198
BS02	GAX	C	S174 Q177 M181 E216 F254 P255 F256 T257 G288 A289 A311 G313	S94 Q97 M101 E136 F174 P175 F176 T177 G208 A209 A231 G233

Gene Ontology

Molecular Function

• GO:0000049 tRNA binding
• GO:0000166 nucleotide binding
• GO:0004812 aminoacyl-tRNA ligase activity
• GO:0004826 phenylalanine-tRNA ligase activity
• GO:0005524 ATP binding

Biological Process

• GO:0006432 phenylalanyl-tRNA aminoacylation
• GO:0043039 tRNA aminoacylation

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2rhs, PDBe:2rhs, PDBj:2rhs
• PDBsum: 2rhs
• PubMed: 18086534
• UniProt: Q4L5E3|SYFA_STAHJ Phenylalanine--tRNA ligase alpha subunit (Gene Name=pheS)