Structure of PDB 3p0h Chain B

Receptor sequence

>3p0hB (length=598) Species: 5664 (Leishmania major)

HHHMNTDERYKLLRSVGEECIQESELRNLIEKKPLIRCYDGFEPSGRMHI
AQGIFKAVNVNKCTAAGCEFVFWVADWFALMNDGGELEKIRIVGRYLIEV
WKAAGMDMDKVLFLWSSEEITSHADTYWRMVLDIGRQNTIARIKKCCGTL
TAAQVLYPLMQCCDIFFLKADICQLGLDQRKVNMLAREYCDLIGRKLKPV
ILSHHMLAGLKQGQAKMSKSDPDSAIFMEDTEEDVARKIRQAYCPRVKQS
ASAITDDGAPVATDDRNPVLDYFQCVVYARPGAAATIDGTTYATYEDLEQ
AFVSDEVSEDALKSCLIDEVNALLEPVRQHFASNEEAHELLEAVKSYRKA
LPAAPAKPHACMWMPALLKVPLDVAEGMIKVTKDFIAAHPEGTVTLVLPD
WSAVASDEITGVEKDISAALQVNCALLKAYGLPSSVKIVTENEVILGNCD
DFWVSVIGIARKNLLSHVEELYGGEVRNAGQVIAALMRVATALMLSVSHV
ISTSLDGHINAFAREYTKERIDCVQTLEGDDVLYLDDNDMDIRRKIKKAV
ISVAQHLLAAAVLQLLLDRSAQARALLNGELKKNMTVLRNAEKKMAKK

3D structure

• PDB: 3p0h The Double-Length Tyrosyl-tRNA Synthetase from the Eukaryote Leishmania major Forms an Intrinsically Asymmetric Pseudo-Dimer.
• Chain: B
• Resolution: 3.0 Å

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	FSE	B	Y36 D37 G38 W70 Q167 D170 L181 G182 D184 Q185	Y39 D40 G41 W73 Q161 D164 L175 G176 D178 Q179

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

External links

• PDB: RCSB:3p0h, PDBe:3p0h, PDBj:3p0h
• PDBsum: 3p0h
• PubMed: 21420975
• UniProt: Q4QFJ7