Structure of PDB 1nyr Chain A

Receptor sequence
>1nyrA (length=642) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
INIQFPDGNKKAFDKGTTTEDIAQSISPGLRKKAVAGKFNGQLVDLTKPL
ETDGSIEIVTPGSEEALEVLRHSTAHLMAHAIKRLYGNVKFGVGPVIEGG
FYYDFDIDQNISSDDFEQIEKTMKQIVNENMKIERKVVSRDEAKELFSND
EYKLELIDAIPEDENVTLYSQGDFTDLCRGVHVPSTAKIKEFKLLSTAGA
YWRGDSNNKMLQRIYGTAFFDKKELKAHLQMLEERKERDHRKIGKELELF
TNSQLVGAGLPLWLPNGATIRREIERYIVDKEVSMGYDHVYTPVLANVDL
YKTSGHWDHYQEDMFPPMQLDETESMVLRPMNCPHHMMIYANKPHSYREL
PIRIAELGTMHRYEASGAVSGLQRVRGMTLNDSHIFVRPDQIKEEFKRVV
NMIIDVYKDFGFEDYSFRLSYRDPEDKEKYFDDDDMWNKAENMLKEAADE
LGLSYEEAIGEAAFYGPKLDVQVKTAMGKEETLSTAQLDFLLPERFDLTY
IGQDGEHHRPVVIHRGVVSTMERFVAFLTEETKGAFPTWLAPKQVQIIPV
NVDLHYDYARQLQDELKSQGVRVSIDDRNEKMGYKIREAQMQKIPYQIVV
GDKEVENNQVNVRQYGSQDQETVEKDEFIWNLVDEIRLKKHR
3D structure
PDB1nyr Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C336 R365 L383 D385 H387 K471 H517
Catalytic site (residue number reindexed from 1) C333 R362 L380 D382 H384 K468 H514
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 C336 H387 H517 C333 H384 H514
BS02 ZN A H75 H79 C181 H185 H72 H76 C178 H182
BS03 ATP A R365 E367 R377 V378 M381 T485 L486 T523 R526 R362 E364 R374 V375 M378 T482 L483 T520 R523
BS04 THR A M334 C336 D385 H387 H517 M331 C333 D382 H384 H514
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:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006435 threonyl-tRNA aminoacylation
GO:0043039 tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1nyr, PDBe:1nyr, PDBj:1nyr
PDBsum1nyr
PubMed12875846
UniProtQ8NW68|SYT_STAAW Threonine--tRNA ligase (Gene Name=thrS)

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