3A5Y

Crystal structure of GenX from Escherichia coli in complex with lysyladenylate analog

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004824	molecular_function	lysine-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	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006430	biological_process	lysyl-tRNA aminoacylation
A	0016874	molecular_function	ligase activity
A	0016880	molecular_function	acid-ammonia (or amide) ligase activity
A	0042803	molecular_function	protein homodimerization activity
A	0043687	biological_process	post-translational protein modification
A	0052868	molecular_function	protein-lysine lysyltransferase activity
A	0071468	biological_process	cellular response to acidic pH
B	0000049	molecular_function	tRNA binding
B	0000166	molecular_function	nucleotide binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004824	molecular_function	lysine-tRNA ligase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006430	biological_process	lysyl-tRNA aminoacylation
B	0016874	molecular_function	ligase activity
B	0016880	molecular_function	acid-ammonia (or amide) ligase activity
B	0042803	molecular_function	protein homodimerization activity
B	0043687	biological_process	post-translational protein modification
B	0052868	molecular_function	protein-lysine lysyltransferase activity
B	0071468	biological_process	cellular response to acidic pH
C	0000049	molecular_function	tRNA binding
C	0000166	molecular_function	nucleotide binding
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004824	molecular_function	lysine-tRNA ligase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006418	biological_process	tRNA aminoacylation for protein translation
C	0006430	biological_process	lysyl-tRNA aminoacylation
C	0016874	molecular_function	ligase activity
C	0016880	molecular_function	acid-ammonia (or amide) ligase activity
C	0042803	molecular_function	protein homodimerization activity
C	0043687	biological_process	post-translational protein modification
C	0052868	molecular_function	protein-lysine lysyltransferase activity
C	0071468	biological_process	cellular response to acidic pH
D	0000049	molecular_function	tRNA binding
D	0000166	molecular_function	nucleotide binding
D	0004812	molecular_function	aminoacyl-tRNA ligase activity
D	0004824	molecular_function	lysine-tRNA ligase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006418	biological_process	tRNA aminoacylation for protein translation
D	0006430	biological_process	lysyl-tRNA aminoacylation
D	0016874	molecular_function	ligase activity
D	0016880	molecular_function	acid-ammonia (or amide) ligase activity
D	0042803	molecular_function	protein homodimerization activity
D	0043687	biological_process	post-translational protein modification
D	0052868	molecular_function	protein-lysine lysyltransferase activity
D	0071468	biological_process	cellular response to acidic pH

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE KAA A 1990

Chain	Residue
A	SER76
A	GLU244
A	LEU245
A	ALA246
A	ASN247
A	PHE249
A	GLU251
A	GLY296
A	ALA298
A	GLY300
A	ARG303
A	GLU78
A	LEU314
A	HOH394
A	HOH409
A	HOH478
A	HOH563
A	ARG100
A	GLU102
A	HIS108
A	ASN109
A	PHE112
A	MET114
A	TYR118

---

site_id	AC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE KAA B 1991

Chain	Residue
B	SER76
B	GLU78
B	ARG100
B	GLU102
B	HIS108
B	ASN109
B	PHE112
B	MET114
B	TYR118
B	GLU244
B	LEU245
B	ALA246
B	ASN247
B	PHE249
B	GLU251
B	GLY296
B	ALA298
B	GLY300
B	ARG303
B	LEU314
B	HOH399
B	HOH404
B	HOH428
B	HOH429
B	HOH495
B	HOH553

---

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE KAA C 1992

Chain	Residue
C	GLU78
C	ARG100
C	GLU102
C	HIS108
C	ASN109
C	PHE112
C	MET114
C	TYR118
C	GLU244
C	LEU245
C	ALA246
C	ASN247
C	PHE249
C	GLU251
C	GLY296
C	ALA298
C	GLY300
C	ARG303
C	LEU314
C	HOH646
C	HOH683
C	HOH693
C	HOH742
C	HOH746
C	HOH758
C	HOH799

---

site_id	AC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE KAA D 1993

Chain	Residue
D	HOH920
D	HOH950
D	HOH1001
D	SER76
D	GLU78
D	ARG100
D	GLU102
D	TYR107
D	HIS108
D	ASN109
D	PHE112
D	MET114
D	TYR118
D	GLU244
D	LEU245
D	ALA246
D	ASN247
D	PHE249
D	GLU251
D	GLY296
D	ALA298
D	GLY300
D	ARG303
D	HOH867
D	HOH905
D	HOH916

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {}

Chain

Residue

Details

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