Structure of PDB 3p0j Chain D

Receptor sequence
>3p0jD (length=665) Species: 5664 (Leishmania major) [Search protein sequence]
HHMNTDERYKLLRSVGEECIQESELRNLIEKKPLIRCYDGFEPSGRMHIA
QGIFKAVNVNKCTAAGCEFVFWVADWFALMNDKVGGELEKIRIVGRYLIE
VWKAAGMDMDKVLFLWSSEEITSHADTYWRMVLDIGRQNTIARIKKCCTI
MGKTEGTLTAAQVLYPLMQCCDIFFLKADICQLGLDQRKVNMLAREYCDL
IGRKLKPVILSHHMLAGLKQGQAKMSKSDPDSAIFMEDTEEDVARKIRQA
YCPRVKQSASAITDDGAPVATDDRNPVLDYFQCVVYARPGAAATIDGTTY
ATYEDLEQAFVSDEVSEDALKSCLIDEVNALLEPVRQHFASNEEAHELLE
AVKSYRALPAAPAKPHACMWMPALLKVPLDVAEGMIKVTKDFIAAHPEGT
VTLVLPDWSAVASDEITGVEKDISAALQVNCALLKAYGLPSSVKIVTENE
VILGNCDDFWVSVIGIARKNLLSHVEELYGGEVRNAGQVIAALMRVATAL
MLSVSHVISTSLDGHINAFAREYTKERIDCVQTLEGRIPALHRPGADDVL
YLDDNDMDIRRKIKKAYSAPNEEANPVISVAQHLLAQHGALSIERGEANG
GNVSYNTPEALVADCGSGALHPADLKAAVLQLLLDRSAQARALLNGELKK
NMTVLRNAEKKMAKK
3D structure
PDB3p0j The Double-Length Tyrosyl-tRNA Synthetase from the Eukaryote Leishmania major Forms an Intrinsically Asymmetric Pseudo-Dimer.
ChainD
Resolution2.89 Å
3D
structure
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Enzymatic activity
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 TYE D Y36 G38 W70 F75 Q167 D170 L181 Q185 Y38 G40 W72 F77 Q169 D172 L183 Q187
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:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006437 tyrosyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0097014 ciliary plasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3p0j, PDBe:3p0j, PDBj:3p0j
PDBsum3p0j
PubMed21420975
UniProtQ4QFJ7

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