Structure of PDB 1vbn Chain B

Receptor sequence
>1vbnB (length=318) Species: 562 (Escherichia coli) [Search protein sequence]
NLIKQLQERGLVAQVTDEEALAERLAQGPIALVCGFDPTADSLHLGHLVP
LLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEWVDKI
RKQVAPFLDFDCGENSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINK
EAVKQRLNREDQGISFTEFSYNLLQGYDFACLNKQYGVVLCIGGSDQWGN
ITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAVWLDPKKTSPY
KFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDKNSGKAPRAQYVLA
EQVTRLVHGEEGLQAAKR
3D structure
PDB1vbn Structural basis of nonnatural amino acid recognition by an engineered aminoacyl-tRNA synthetase for genetic code expansion
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T43 H48 H51 K85 R89 Q179 D200 K235 K238 T239
Catalytic site (residue number reindexed from 1) T39 H44 H47 K81 R85 Q175 D196 K231 K234 T235
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 B G39 G50 H51 P54 L71 D81 Y175 Q179 D182 G198 D200 Q201 L227 G35 G46 H47 P50 L67 D77 Y171 Q175 D178 G194 D196 Q197 L223 BindingDB: Ki=2.9nM
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:1vbn, PDBe:1vbn, PDBj:1vbn
PDBsum1vbn
PubMed15671170
UniProtP0AGJ9|SYY_ECOLI Tyrosine--tRNA ligase (Gene Name=tyrS)

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