1ZJW

Glutaminyl-tRNA synthetase complexed to glutamine and 2'deoxy A76 glutamine tRNA

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	0043039	biological_process	tRNA aminoacylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1394

Chain	Residue
A	HIS40
A	HIS43
A	ARG260
A	MET268
A	LYS270
A	AMP998

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1395

Chain	Residue
A	LYS272
A	GLY482
A	HOH1472
A	VAL267
A	MET268
A	SER269

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site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE AMP A 998

Chain	Residue
A	PRO33
A	GLU34
A	GLY42
A	HIS43
A	SER46
A	THR230
A	ARG260
A	LEU261
A	LYS270
A	GLN996
A	SO41394
A	HOH1447
A	HOH1477

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site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GLN A 996

Chain	Residue
A	PRO32
A	TYR211
A	HIS215
A	CYS229
A	PHE233
A	AMP998
A	HOH1396
A	HOH1476
A	HOH1477
B	A976

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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	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:23727144, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ

Chain	Residue	Details
A	PRO35
A	ILE41

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:1O0B

Chain	Residue	Details
A	ASP67

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:15845536, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:1O0B, ECO:0007744|PDB:1ZJW

Chain	Residue	Details
A	ASP212

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site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ

Chain	Residue	Details
A	LEU231
A	LEU261
A	SER269

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1euy

Chain	Residue	Details
A	GLU34
A	LYS270
A	ARG260

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1euy

Chain	Residue	Details
A	LYS270

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site_id	MCSA1
Number of Residues	3
Details	M-CSA 850

Chain	Residue	Details
A	PRO35	proton shuttle (general acid/base)
A	LEU261	electrostatic stabiliser
A	ARG271	electrostatic stabiliser

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