Structure of PDB 1x8x Chain A

Receptor sequence
>1x8xA (length=322) Species: 562 (Escherichia coli) [Search protein sequence]
MASSNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHLG
HLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEW
VDKIRKQVAPFLDFDCGENSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQ
MINKEAVKQRLNREDQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSD
QWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAVWLDPKK
TSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDKNSGKAPRAQ
YVLAEQVTRLVHGEEGLQAAKR
3D structure
PDB1x8x Structural Snapshots of the KMSKS Loop Rearrangement for Amino Acid Activation by Bacterial Tyrosyl-tRNA Synthetase
ChainA
Resolution2.0 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) T43 H48 H51 K85 R89 Q179 D200 K235 K238 T239
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 TYR A Y37 G39 D81 Y175 Q179 D182 Q201 Y37 G39 D81 Y175 Q179 D182 Q201
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:1x8x, PDBe:1x8x, PDBj:1x8x
PDBsum1x8x
PubMed15663931
UniProtP0AGJ9|SYY_ECOLI Tyrosine--tRNA ligase (Gene Name=tyrS)

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