Structure of PDB 2rhq Chain A

Receptor sequence

>2rhqA (length=270) Species: 1283 (Staphylococcus haemolyticus)

LMEKLNQQLAEETIDVTLPSRQISIGSKHPLTRTVEEIEDLFLGLGYEIV
DGYEVEQDYYNFEALNLPKSHPARDMQDSFYITDEILMRTHTSPVQARTM
EKRNGQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMSDLKG
TLELVAKKLFGADREIRLRPSYFPFTEPSVEVDVSCFKCKGKGCNVCKHT
GWIEILGAGMVHPNVLEMAGFDSNEYSGFAFGMGPDRIAMLKYGIEDIRY
FYTNDVRFLEQFKAVEDRGE

3D structure

• PDB: 2rhq Rational protein engineering in action: the first crystal structure of a phenylalanine tRNA synthetase from Staphylococcus haemolyticus.
• Chain: A
• 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): Q77 H91 R119 Q133 T176 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	ZN	A	C267 C270 C275 C278	C186 C189 C194 C197
BS02	GAX	A	S174 Q177 M181 Q214 E216 F254 F256 T257 G288 A289 A311 G313	S93 Q96 M100 Q133 E135 F173 F175 T176 G207 A208 A230 G232

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