8H99

Crystal structure of E. coli ThrS catalytic domain mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004829	molecular_function	threonine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006435	biological_process	threonyl-tRNA aminoacylation
B	0000166	molecular_function	nucleotide binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004829	molecular_function	threonine-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006435	biological_process	threonyl-tRNA aminoacylation

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	582
Details	Region: {"description":"Catalytic","evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10881191","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11136973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11953757","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10881191","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11136973","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	107
Details	Region: {"description":"Anticodon recognition","evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11953757","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QF6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI9
Number of Residues	58
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

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

---

site_id	MCSA2
Number of Residues	7
Details	M-CSA 540

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

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