Structure of PDB 4yye Chain A

Receptor sequence
>4yyeA (length=418) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
ATMTSMVSQRQDLFMTDPLSPGSMFFLPNGAKIFNKLIEFMKLQQKFKFG
FNEVVTPLIYKKTLWEKSGHWENYADDMFKVETTDEEKEEYGLKPMNCPG
HCLIFGKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHI
FCTPSQVKSEIFNSLKLIDIVYNKIFPSNYFINFSTRPDHFIGDLKVWNH
AEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTDHLRKTHQVATIQLD
FQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFW
LNPYQAVIIPVNTKNVQQLDMCTALQKKLRNELEADDMEPVPLNDWHFNV
DLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNRKSFEK
LTMSQIWEKFIELEKNYK
3D structure
PDB4yye The crystal structure of yeast mitochondrial ThrRS in complex with the canonical threonine tRNA.
ChainA
Resolution2.301 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C133 R162 Q180 D182 H184 K273 H319
Catalytic site (residue number reindexed from 1) C98 R127 Q145 D147 H149 K229 H275
Enzyme Commision number 6.1.1.3: threonine--tRNA ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004829 threonine-tRNA ligase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0140101 catalytic activity, acting on a tRNA
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006435 threonyl-tRNA aminoacylation
GO:0070159 mitochondrial threonyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4yye, PDBe:4yye, PDBj:4yye
PDBsum4yye
PubMed26704982
UniProtP07236|SYTM_YEAST Threonine--tRNA ligase, mitochondrial (Gene Name=MST1)

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