Structure of PDB 3l4g Chain G

Receptor sequence
>3l4gG (length=309) Species: 9606 (Homo sapiens) [Search protein sequence]
QETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQI
FLEMGFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEALQ
LPMDYVQRVKRTHSQGGYGSQGYKYNWKLDEARKNLLRTHTTSASARALY
RLAQKKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHL
MGVLREFFTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGV
FRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKVNLQMV
YDSPLCRLD
3D structure
PDB3l4g Structure of human cytosolic phenylalanyl-tRNA synthetase: evidence for kingdom-specific design of the active sites and tRNA binding patterns.
ChainG
Resolution3.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H274 H327 R358 Q372 T413 A456
Catalytic site (residue number reindexed from 1) H87 H140 R171 Q185 T226 A269
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 PHE G T329 E374 N434 S435 A456 G458 T142 E187 N247 S248 A269 G271
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0003723 RNA binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004826 phenylalanine-tRNA ligase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006432 phenylalanyl-tRNA aminoacylation
GO:0043039 tRNA aminoacylation
GO:0051290 protein heterotetramerization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009328 phenylalanine-tRNA ligase complex
GO:0016020 membrane

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Cellular Component
External links
PDB RCSB:3l4g, PDBe:3l4g, PDBj:3l4g
PDBsum3l4g
PubMed20223217
UniProtQ9Y285|SYFA_HUMAN Phenylalanine--tRNA ligase alpha subunit (Gene Name=FARSA)

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