Structure of PDB 2pid Chain A

Receptor sequence
>2pidA (length=317) Species: 9606 (Homo sapiens) [Search protein sequence]
GLLAAQKARGLFKDFFPETGTKIELPELFPQTIYCGFDPTADSLHVGHLL
ALLGLFHLQRAGHNVIALVGGATARLGDPSGRTKEREALETERVRANARA
LRLGLEALAANHQQLFTDGRSWGSFTVLDNSAWYQKQHLVDFLAAVGGHF
RMGTLLSRQSVQLRLKSPEGMSLAEFFYQVLQAYDFYYLFQRYGCRVQLG
GSDQLGNIMSGYEFINKLTGEDVFGITVPLITAVWLNRDKTSPFELYQFF
VRQPDDSVERYLKLFTFLPLPEIDHIMQLHVKEPERRGPQKRLAAEVTKL
VHGREGLDSAKRCTQAL
3D structure
PDB2pid Crystal Structure of Human Mitochondrial Tyrosyl-tRNA Synthetase Reveals Common and Idiosyncratic Features.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T83 H88 H91 R125 R129 Q225 D246
Catalytic site (residue number reindexed from 1) T40 H45 H48 R82 R86 Q182 D203
Enzyme Commision number 6.1.1.1: tyrosine--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 YSA A Y77 G79 D81 G90 H91 Y221 Q225 D228 G243 G244 D246 Q247 L273 I274 Y34 G36 D38 G47 H48 Y178 Q182 D185 G200 G201 D203 Q204 L230 I231
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004831 tyrosine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006437 tyrosyl-tRNA aminoacylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2pid, PDBe:2pid, PDBj:2pid
PDBsum2pid
PubMed17997975
UniProtQ9Y2Z4|SYYM_HUMAN Tyrosine--tRNA ligase, mitochondrial (Gene Name=YARS2)

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