4JXX

Crystal structure of E coli E. coli glutaminyl-tRNA synthetase bound to tRNA(Gln)(CUG) and ATP from novel cryostabilization conditions

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004819	molecular_function	glutamine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006424	biological_process	glutamyl-tRNA aminoacylation
A	0006425	biological_process	glutaminyl-tRNA aminoacylation
A	0016874	molecular_function	ligase activity
A	0043039	biological_process	tRNA aminoacylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP A 601

Chain	Residue
A	PHE31
A	LEU261
A	MET268
A	LYS270
A	HOH704
A	HOH800
A	HOH814
A	HOH832
A	HOH877
B	A976
A	PRO33
A	GLU34
A	HIS40
A	GLY42
A	HIS43
A	SER46
A	THR230
A	ARG260

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 602

Chain	Residue
A	VAL267
A	MET268
A	SER269

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Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	12
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PepNGyLHIGHA

Chain	Residue	Details
A	PRO33-ALA44

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	Region: {"description":"Interaction with tRNA","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23727144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	10
Details	Motif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Motif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23727144","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JXZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JYZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12691748","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18477696","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O0B","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12691748","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15845536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18477696","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O0B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZJW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18477696","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23727144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JXZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JYZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 850

Chain	Residue	Details
A	GLU34	proton shuttle (general acid/base)
A	ARG260	electrostatic stabiliser
A	LYS270	electrostatic stabiliser

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