Structure of PDB 3ugt Chain D

Receptor sequence
>3ugtD (length=418) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
ATMTSMVSQRQDLFMTDPLSPGSMFFLPNGAKIFNKLIEFMKLQQKFKFG
FNEVVTPLIYKKTLWEKSGHWENYADDMFKVEKEEYGLKPMNCPGHCLIF
GKKDRSYNELPLRFSDFSPLHRNEASGALSGLTRLRKFHQDDGHIFCTPS
QVKSEIFNSLKLIDIVYNKIFPFVKGGSNYFINFSTRPDHFIGDLKVWNH
AEQVLKEILEESGKPWKLNPGDGAFYGPKLDIMVTDHLRKTHQVATIQLD
FQLPERFDLKFKDQDNSYKRPIMIHRATFGSIERFMALLIDSNEGRWPFW
LNPYQAVIIPVNTKNVQQLDMCTALQKKLRNELEADDMEPVPLNDWHFNV
DLDIRNEPVGYRIKSAILKNYSYLIIVGDEEVQLQKYNIRERDNRKSFEK
LTMSQIWEKFIELEKNYK
3D structure
PDB3ugt Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment.
ChainD
Resolution3.6 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) C93 R122 Q140 D142 H144 K229 H275
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 D H184 H319 H144 H275
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:3ugt, PDBe:3ugt, PDBj:3ugt
PDBsum3ugt
PubMed22343532
UniProtP07236|SYTM_YEAST Threonine--tRNA ligase, mitochondrial (Gene Name=MST1)

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