1LYL

LYSYL-TRNA SYNTHETASE (LYSU) (E.C.6.1.1.6) COMPLEXED WITH LYSINE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0003676	molecular_function	nucleic acid binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004824	molecular_function	lysine-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	0006430	biological_process	lysyl-tRNA aminoacylation
A	0016020	cellular_component	membrane
A	0016874	molecular_function	ligase activity
A	0034605	biological_process	cellular response to heat
A	0036260	biological_process	RNA capping
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
B	0000049	molecular_function	tRNA binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003676	molecular_function	nucleic acid binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004824	molecular_function	lysine-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006430	biological_process	lysyl-tRNA aminoacylation
B	0016020	cellular_component	membrane
B	0016874	molecular_function	ligase activity
B	0034605	biological_process	cellular response to heat
B	0036260	biological_process	RNA capping
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
C	0000049	molecular_function	tRNA binding
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003676	molecular_function	nucleic acid binding
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004824	molecular_function	lysine-tRNA ligase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0006418	biological_process	tRNA aminoacylation for protein translation
C	0006430	biological_process	lysyl-tRNA aminoacylation
C	0016020	cellular_component	membrane
C	0016874	molecular_function	ligase activity
C	0034605	biological_process	cellular response to heat
C	0036260	biological_process	RNA capping
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE LYS A 505

Chain	Residue
A	GLY216
A	GLY473
A	GLU240
A	ARG262
A	MET276
A	GLU278
A	TYR280
A	ASN424
A	PHE426
A	GLU428

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE LYS B 505

Chain	Residue
B	GLY216
B	ALA238
B	GLU240
B	ARG262
B	GLU278
B	TYR280
B	ASN424
B	PHE426
B	GLU428
B	GLY473

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE LYS C 505

Chain	Residue
C	GLY216
C	GLU240
C	GLU278
C	TYR280
C	ASN424
C	PHE426
C	GLU428
C	GLY473
C	GLY475

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG480
A	GLU278
A	ARG262

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1asy

Chain	Residue	Details
B	ARG480
B	GLU278
B	ARG262

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1asy

Chain	Residue	Details
C	ARG480
C	GLU278
C	ARG262

---

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1asy

Chain	Residue	Details
A	ARG262

---

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1asy

Chain	Residue	Details
B	ARG262

---

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1asy

Chain	Residue	Details
C	ARG262

---