Structure of PDB 2rhs Chain A

Receptor sequence
>2rhsA (length=249) Species: 1283 (Staphylococcus haemolyticus) [Search protein sequence]
NQQLAEETIDVTLPSRQISIGSKHPLTRTVEEIEDLFLGLGYEIVDGYEV
EQDYYNFEALNLPKSHPARDMQDSFYITDEILMRTHTSPVQARTMEKRNG
QGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMSDLKGTLELV
AKKLFGADREIRLRPSYFPFTEPSVEVDVSWIEILGAGMVHPNVLEMAGF
DSNEYSGFAFGMGPDRIAMLKYGIEDIRYFYTNDVRFLEQFKAVEDRGE
3D structure
PDB2rhs Rational protein engineering in action: the first crystal structure of a phenylalanine tRNA synthetase from Staphylococcus haemolyticus.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q158 H172 R200 Q214 T257 A311
Catalytic site (residue number reindexed from 1) Q72 H86 R114 Q128 T171 A209
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 GAX A S174 Q177 E216 F254 P255 F256 T257 G288 A289 A311 G313 S88 Q91 E130 F168 P169 F170 T171 G186 A187 A209 G211
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

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Cellular Component
External links
PDB RCSB:2rhs, PDBe:2rhs, PDBj:2rhs
PDBsum2rhs
PubMed18086534
UniProtQ4L5E3|SYFA_STAHJ Phenylalanine--tRNA ligase alpha subunit (Gene Name=pheS)

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