Structure of PDB 1n78 Chain B

Receptor sequence

>1n78B (length=468) Species: 274 (Thermus thermophilus) [Search protein sequence]

MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVP
GAEERILAALKWLGLSYDEGPDVGGPHGPYRQSERLPLYQKYAEELLKRG
WAYRAFETPEELEQIRKEKGGYDGRARNIPPEEAEERARRGEPHVIRLKV
PRPGTTEVKDELRGVVVYDNQEIPDVVLLKSDGYPTYHLANVVDDHLMGV
TDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPDKTKISKRKSH
TSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL
GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRR
AVELMRPRFDTLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPR
LRAQEEWTEAALEALLRGFAAEKGVKLGQVAQPLRAALTGSLETPGLFEI
LALLGKERALRRLERALA

3D structure

PDB

1n78 ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding

Chain

Resolution

2.1 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	K246
Catalytic site (residue number reindexed from 1)	K246
Enzyme Commision number	6.1.1.17: glutamate--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	rna	B	S9 T43 R47 V145 R163 V166 Y168 E172 V177 K180 S181 Y187 E207 E208 W209 L210 R237 K241 T242 K243 G274 E282 L300 P303 V304 E308 K309 W312 R319 P357 R358 R417 L427 Q432 R435 L442 E443 T444 G446 L447 F448	S9 T43 R47 V145 R163 V166 Y168 E172 V177 K180 S181 Y187 E207 E208 W209 L210 R237 K241 T242 K243 G274 E282 L300 P303 V304 E308 K309 W312 R319 P357 R358 R417 L427 Q432 R435 L442 E443 T444 G446 L447 F448	PDBbind-CN: Ki=3uM
BS02	GOM	B	R5 A7 S9 G17 T18 I21 E41 Y187 N191 R205 A206 W209 L235 L236	R5 A7 S9 G17 T18 I21 E41 Y187 N191 R205 A206 W209 L235 L236

Gene Ontology

	Molecular Function
GO:0000049	tRNA binding
GO:0000166	nucleotide binding
GO:0004812	aminoacyl-tRNA ligase activity
GO:0004818	glutamate-tRNA ligase activity
GO:0005524	ATP binding
GO:0008270	zinc ion binding

	Biological Process
GO:0006412	translation
GO:0006418	tRNA aminoacylation for protein translation
GO:0006424	glutamyl-tRNA aminoacylation
GO:0043039	tRNA aminoacylation

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:1n78, PDBe:1n78, PDBj:1n78
PDBsum	1n78
PubMed	12554668
UniProt	P27000\|SYE_THET8 Glutamate--tRNA ligase (Gene Name=gltX)

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