Structure of PDB 1nyq Chain A

Receptor sequence
>1nyqA (length=642) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
INIQFPDGNKKAFDKGTTTEDIAQSISPGLRKKAVAGKFNGQLVDLTKPL
ETDGSIEIVTPGSEEALEVLRHSTAHLMAHAIKRLYGNVKFGVGPVIEGG
FYYDFDIDQNISSDDFEQIEKTMKQIVNENMKIERKVVSRDEAKELFSND
EYKLELIDAIPEDENVTLYSQGDFTDLCRGVHVPSTAKIKEFKLLSTAGA
YWRGDSNNKMLQRIYGTAFFDKKELKAHLQMLEERKERDHRKIGKELELF
TNSQLVGAGLPLWLPNGATIRREIERYIVDKEVSMGYDHVYTPVLANVDL
YKTSGHWDHYQEDMFPPMQLDETESMVLRPMNCPHHMMIYANKPHSYREL
PIRIAELGTMHRYEASGAVSGLQRVRGMTLNDSHIFVRPDQIKEEFKRVV
NMIIDVYKDFGFEDYSFRLSYRDPEDKEKYFDDDDMWNKAENMLKEAADE
LGLSYEEAIGEAAFYGPKLDVQVKTAMGKEETLSTAQLDFLLPERFDLTY
IGQDGEHHRPVVIHRGVVSTMERFVAFLTEETKGAFPTWLAPKQVQIIPV
NVDLHYDYARQLQDELKSQGVRVSIDDRNEKMGYKIREAQMQKIPYQIVV
GDKEVENNQVNVRQYGSQDQETVEKDEFIWNLVDEIRLKKHR
3D structure
PDB1nyq Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase
ChainA
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 TSB A M334 R365 R377 V378 M381 L383 D385 H387 Y468 T485 Q490 H517 T523 R526 M331 R362 R374 V375 M378 L380 D382 H384 Y465 T482 Q487 H514 T520 R523
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1nyq, PDBe:1nyq, PDBj:1nyq
PDBsum1nyq
PubMed12875846
UniProtQ8NW68|SYT_STAAW Threonine--tRNA ligase (Gene Name=thrS)

[Back to BioLiP]