Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6AQG

Crystal Structure of Lysyl-tRNA Synthetase from Mycobacterium ulcerans complexed with L-lysine and Cladosporin

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	0003877	molecular_function	ATP:ADP adenylyltransferase activity
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004824	molecular_function	lysine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005615	cellular_component	extracellular space
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	0015966	biological_process	diadenosine tetraphosphate biosynthetic process
A	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
A	0043032	biological_process	positive regulation of macrophage activation
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	0003877	molecular_function	ATP:ADP adenylyltransferase activity
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004824	molecular_function	lysine-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0005615	cellular_component	extracellular space
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	0015966	biological_process	diadenosine tetraphosphate biosynthetic process
B	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
B	0043032	biological_process	positive regulation of macrophage activation
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	0003877	molecular_function	ATP:ADP adenylyltransferase activity
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004824	molecular_function	lysine-tRNA ligase activity
C	0005524	molecular_function	ATP binding
C	0005615	cellular_component	extracellular space
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	0015966	biological_process	diadenosine tetraphosphate biosynthetic process
C	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
C	0043032	biological_process	positive regulation of macrophage activation
C	0046872	molecular_function	metal ion binding
D	0000049	molecular_function	tRNA binding
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003676	molecular_function	nucleic acid binding
D	0003877	molecular_function	ATP:ADP adenylyltransferase activity
D	0004812	molecular_function	aminoacyl-tRNA ligase activity
D	0004824	molecular_function	lysine-tRNA ligase activity
D	0005524	molecular_function	ATP binding
D	0005615	cellular_component	extracellular space
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006412	biological_process	translation
D	0006418	biological_process	tRNA aminoacylation for protein translation
D	0006430	biological_process	lysyl-tRNA aminoacylation
D	0015966	biological_process	diadenosine tetraphosphate biosynthetic process
D	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
D	0043032	biological_process	positive regulation of macrophage activation
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue LYS A 601

Chain	Residue
A	GLY209
A	HOH706
A	HOH752
A	HOH892
A	ALA210
A	GLU233
A	ARG255
A	GLU271
A	TYR273
A	TYR420
A	GLU422
A	GLY467

site_id	AC2
Number of Residues	12
Details	binding site for residue KRS A 602

Chain	Residue
A	THR262
A	HIS263
A	SER264
A	PHE267
A	MET269
A	LEU416
A	GLY469
A	GLY471
A	ARG474
A	ILE484
A	HOH739
A	HOH763

site_id	AC3
Number of Residues	6
Details	binding site for residue MPD A 603

Chain	Residue
A	GLY242
A	GLY243
A	PHE244
D	GLY83
D	ASP84
D	ARG173

site_id	AC4
Number of Residues	4
Details	binding site for residue MPD A 604

Chain	Residue
A	GLU257
A	GLY258
A	ASP260
A	HIS263

site_id	AC5
Number of Residues	5
Details	binding site for residue MPD A 605

Chain	Residue
A	VAL67
A	PHE68
A	PRO147
A	VAL148
A	VAL168

site_id	AC6
Number of Residues	12
Details	binding site for residue LYS B 601

Chain	Residue
B	GLY209
B	GLU233
B	ARG255
B	GLU271
B	TYR273
B	TYR420
B	GLU422
B	GLY467
B	KRS602
B	HOH710
B	HOH803
B	HOH868

site_id	AC7
Number of Residues	13
Details	binding site for residue KRS B 602

Chain	Residue
B	ARG255
B	THR262
B	HIS263
B	SER264
B	PHE267
B	LEU416
B	GLY469
B	GLY471
B	ARG474
B	ILE484
B	LYS601
B	HOH777
B	HOH795

site_id	AC8
Number of Residues	5
Details	binding site for residue MPD B 603

Chain	Residue
B	GLY83
B	ASP84
C	GLY242
C	GLY243
C	PHE244

site_id	AC9
Number of Residues	3
Details	binding site for residue MPD B 604

Chain	Residue
B	GLU257
B	GLY258
B	HIS263

site_id	AD1
Number of Residues	6
Details	binding site for residue MPD B 605

Chain	Residue
A	GLY331
A	GLU332
B	GLU332
B	GLN333
B	HOH769
B	HOH863

site_id	AD2
Number of Residues	1
Details	binding site for residue MPD B 606

Chain	Residue
B	HOH722

site_id	AD3
Number of Residues	11
Details	binding site for residue LYS C 601

Chain	Residue
C	GLY209
C	ALA210
C	GLU233
C	ARG255
C	GLU271
C	TYR273
C	TYR420
C	GLU422
C	GLY467
C	KRS602
C	HOH716

site_id	AD4
Number of Residues	13
Details	binding site for residue KRS C 602

Chain	Residue
C	GLY471
C	ARG474
C	LYS601
C	HOH723
C	GLU257
C	THR262
C	HIS263
C	SER264
C	PHE267
C	MET269
C	GLU415
C	THR418
C	GLY469

site_id	AD5
Number of Residues	6
Details	binding site for residue MPD C 603

Chain	Residue
B	LEU196
B	GLY242
B	GLY243
B	PHE244
C	GLY83
C	ASP84

site_id	AD6
Number of Residues	6
Details	binding site for residue MPD D 501

Chain	Residue
A	GLY83
A	ASP84
A	ARG177
D	GLY242
D	GLY243
D	PHE244

site_id	AD7
Number of Residues	11
Details	binding site for residue LYS D 502

Chain	Residue
D	GLY209
D	GLU233
D	ARG255
D	MET269
D	GLU271
D	TYR273
D	TYR420
D	GLU422
D	GLY467
D	KRS503
D	HOH649

site_id	AD8
Number of Residues	12
Details	binding site for residue KRS D 503

Chain	Residue
D	GLU257
D	THR262
D	HIS263
D	SER264
D	PHE267
D	MET269
D	GLU415
D	THR418
D	GLY469
D	ARG474
D	LYS502
D	HOH702

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)