1QF6

STRUCTURE OF E. COLI THREONYL-TRNA SYNTHETASE COMPLEXED WITH ITS COGNATE TRNA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0000166	molecular_function	nucleotide binding
A	0000900	molecular_function	mRNA regulatory element binding translation repressor activity
A	0002161	molecular_function	aminoacyl-tRNA editing activity
A	0003723	molecular_function	RNA binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004829	molecular_function	threonine-tRNA ligase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006417	biological_process	regulation of translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006435	biological_process	threonyl-tRNA aminoacylation
A	0008270	molecular_function	zinc ion binding
A	0042803	molecular_function	protein homodimerization activity
A	0043039	biological_process	tRNA aminoacylation
A	0045947	biological_process	negative regulation of translational initiation
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding
A	0048027	molecular_function	mRNA 5'-UTR binding
A	0106074	biological_process	aminoacyl-tRNA metabolism involved in translational fidelity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1001

Chain	Residue
A	CYS334
A	HIS385
A	HIS511
A	HOH1123

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site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AMP A 1002

Chain	Residue
A	PHE379
A	GLN381
A	GLN479
A	CYS480
A	THR482
A	GLY516
A	SER517
A	ARG520
A	HOH1118
B	A76
A	ARG363
A	GLU365
A	MET374
A	ARG375
A	VAL376

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11953757

Chain	Residue	Details
A	LYS246
A	ASN342
A	LEU489
A	ASP615

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:10319817, ECO:0007744|PDB:1QF6

Chain	Residue	Details
A	HIS309
A	VAL376
A	GLN381
A	GLN479
A	SER517

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site_id	SWS_FT_FI3
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269|PubMed:10319817

Chain	Residue	Details
A	TYR313
A	ILE547
A	ASN575
A	ARG589
A	VAL595
A	ARG609
A	ARG325
A	TYR348
A	ARG363
A	ARG375
A	PHE379
A	TYR462
A	GLN484
A	ARG520

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:10881191, ECO:0000269|PubMed:11136973, ECO:0000269|PubMed:11953757

Chain	Residue	Details
A	CYS334
A	HIS385

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site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:10881191, ECO:0000269|PubMed:11136973

Chain	Residue	Details
A	HIS511

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	LYS286

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 10319817

Chain	Residue	Details
A	ARG363

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site_id	MCSA1
Number of Residues	7
Details	M-CSA 540

Chain	Residue	Details
A	CYS334	electrostatic stabiliser, metal ligand
A	ARG363	electrostatic stabiliser
A	GLN381	electrostatic stabiliser
A	ASP383	electrostatic stabiliser
A	HIS385	metal ligand
A	LYS465	electrostatic stabiliser
A	HIS511	metal ligand

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