Structure of PDB 3a31 Chain A

Receptor sequence
>3a31A (length=465) Species: 56636 (Aeropyrum pernix) [Search protein sequence]
KTHIDYAYELDITVKPDSRVPVFNREFATFTGAGVPLFSLGGGPIRYALA
EVLAKFHARRGYYVVETPIIASTELFKVSGHIEFYRNNMYLFDIEGHEFA
VKPMNCPYHILLFLNEVAKHRSKLPLPFKVFEFGRVHRYEPSGSIYGLLR
VRGFTQDDAHIIVPGGRVIDVVYDVFEEMKLVLERLFKLGVSSETFKVRL
SMSDKSLIGKEFMGSKEEWEGAEEALREAASRINEKYGIDIVELEGEAAF
YGPKLDFIMMVEESGVSKEWQMGTIQFDFNLPRRFRLYDVVREEFGIEEV
YIIHRALLGSIERFLGVYLEHRRGRMPFTLAPIQFAVIAVKTGGEVDREI
EDLASSIAKGLLDKGFRVAVKGSSKTGLSSDVRHIESTAKPAVNVFIGAK
EVREKVLDVRVFDLESMKRRRLAIAYGDAADAVENLAAVAEELESPVRSL
SGQAPRIPADFSFML
3D structure
PDB3a31 Two complementary enzymes for threonylation of tRNA in crenarchaeota: crystal structure of Aeropyrum pernix threonyl-tRNA synthetase lacking a cis-editing domain
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C112 R144 Q162 D164 H166 K260 H310
Catalytic site (residue number reindexed from 1) C106 R138 Q156 D158 H160 K254 H304
Enzyme Commision number 6.1.1.3: threonine--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 C112 H166 H310 C106 H160 H304
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004829 threonine-tRNA ligase activity
GO:0005524 ATP binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006435 threonyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Biological Process
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Cellular Component
External links
PDB RCSB:3a31, PDBe:3a31, PDBj:3a31
PDBsum3a31
PubMed19761773
UniProtQ9YDW0|SYTC_AERPE Threonine--tRNA ligase catalytic subunit (Gene Name=thrS-cat)

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