Structure of PDB 1h3f Chain A

Receptor sequence
>1h3fA (length=403) Species: 262724 (Thermus thermophilus HB27) [Search protein sequence]
GHTPEEALALLKRGAEEIVPEEELLAKLKEGRPLTVKLGADPTRPDLHLG
HAVVLRKMRQFQELGHKVVLIIGDFTRENAKTYVAQAGKILRQEPHLFEL
RYNSEWLEGLTFKEVVRLTSLMTVAQMLEREDFKKRYEAGIPISLHELLY
PFAQAYDSVAIRADVEMGGTDQRFNLLVGREVQRAYGQSPQVCFLMPLLV
GLDGREKMSKSLDNYIGLTEPPEAMFKKLMRVPDPLLPSYFRLLTDLEEE
EIEALLKAGPVPAHRVLARLLTAAYALPQIPPRIDRAFYESLGYAWEAFG
RDKEAGPEEVRRAEARYDEVAKEEIPEVTIPASELKEGRIWVARLFTLAG
LTPSNAEARRLIQNRGLRLDGEVLTDPMLQVDLSRPRILQRGKDRFVRVR
LSD
3D structure
PDB1h3f Class I Tyrosyl-tRNA Synthetase Has a Class II Mode or tRNA Recognition
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T47 H52 H55 Q179 D196 K232 K235 S236
Catalytic site (residue number reindexed from 1) T43 H48 H51 Q154 D171 K207 K210 S211
Enzyme Commision number 6.1.1.1: tyrosine--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 TYE A K41 G43 Q179 D182 Q197 K37 G39 Q154 D157 Q172
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003723 RNA binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004831 tyrosine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006437 tyrosyl-tRNA aminoacylation
GO:0043039 tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h3f, PDBe:1h3f, PDBj:1h3f
PDBsum1h3f
PubMed12110594
UniProtP83453|SYY_THET2 Tyrosine--tRNA ligase (Gene Name=tyrS)

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