Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1MB2

Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Tryptophan in an Open Conformation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004830	molecular_function	tryptophan-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	0006436	biological_process	tryptophanyl-tRNA aminoacylation
A	0016874	molecular_function	ligase activity
B	0000166	molecular_function	nucleotide binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004830	molecular_function	tryptophan-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	0006436	biological_process	tryptophanyl-tRNA aminoacylation
B	0016874	molecular_function	ligase activity
C	0000166	molecular_function	nucleotide binding
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004830	molecular_function	tryptophan-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	0006436	biological_process	tryptophanyl-tRNA aminoacylation
C	0016874	molecular_function	ligase activity
D	0000166	molecular_function	nucleotide binding
D	0004812	molecular_function	aminoacyl-tRNA ligase activity
D	0004830	molecular_function	tryptophan-tRNA ligase activity
D	0005524	molecular_function	ATP binding
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	0006436	biological_process	tryptophanyl-tRNA aminoacylation
D	0016874	molecular_function	ligase activity
E	0000166	molecular_function	nucleotide binding
E	0004812	molecular_function	aminoacyl-tRNA ligase activity
E	0004830	molecular_function	tryptophan-tRNA ligase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006412	biological_process	translation
E	0006418	biological_process	tRNA aminoacylation for protein translation
E	0006436	biological_process	tryptophanyl-tRNA aminoacylation
E	0016874	molecular_function	ligase activity
F	0000166	molecular_function	nucleotide binding
F	0004812	molecular_function	aminoacyl-tRNA ligase activity
F	0004830	molecular_function	tryptophan-tRNA ligase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006412	biological_process	translation
F	0006418	biological_process	tRNA aminoacylation for protein translation
F	0006436	biological_process	tryptophanyl-tRNA aminoacylation
F	0016874	molecular_function	ligase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRP A 400

Chain	Residue
A	PHE5
A	GLY7
A	VAL40
A	HIS43
A	MET129
A	ASP132
A	VAL143
A	GLN147

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRP B 401

Chain	Residue
B	GLY7
B	GLN9
B	VAL40
B	HIS43
B	MET129
B	ASP132
B	GLN147
B	PHE5

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRP C 402

Chain	Residue
C	PHE5
C	GLY7
C	VAL40
C	HIS43
C	MET129
C	ASP132
C	VAL143
C	GLN147

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRP D 403

Chain	Residue
D	PHE5
D	GLY7
D	GLN9
D	VAL40
D	HIS43
D	MET129
D	ASP132
D	VAL141
D	GLN147

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRP E 404

Chain	Residue
E	PHE5
E	GLY7
E	HIS43
E	MET129
E	ASP132
E	VAL143
E	GLN147

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRP F 405

Chain	Residue
F	PHE5
F	GLY7
F	GLN9
F	HIS43
F	MET129
F	ASP132
F	VAL143
F	GLN147

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	10
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGvITIGNY

Chain	Residue	Details
A	PRO10-TYR19

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	Motif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Motif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	66
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26555258","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DK4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
A	LYS192
A	LYS195

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
B	LYS192
B	LYS195

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
C	LYS192
C	LYS195

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
D	LYS192
D	LYS195

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
E	LYS192
E	LYS195

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
F	LYS192
F	LYS195

site_id	MCSA1
Number of Residues	3
Details	M-CSA 481

Chain	Residue	Details
A	LYS111	electrostatic stabiliser
A	LYS192	electrostatic stabiliser
A	LYS195	electrostatic stabiliser

site_id	MCSA2
Number of Residues	3
Details	M-CSA 481

Chain	Residue	Details
B	LYS111	electrostatic stabiliser
B	LYS192	electrostatic stabiliser
B	LYS195	electrostatic stabiliser

site_id	MCSA3
Number of Residues	3
Details	M-CSA 481

Chain	Residue	Details
C	LYS111	electrostatic stabiliser
C	LYS192	electrostatic stabiliser
C	LYS195	electrostatic stabiliser

site_id	MCSA4
Number of Residues	3
Details	M-CSA 481

Chain	Residue	Details
D	LYS111	electrostatic stabiliser
D	LYS192	electrostatic stabiliser
D	LYS195	electrostatic stabiliser

site_id	MCSA5
Number of Residues	3
Details	M-CSA 481

Chain	Residue	Details
E	LYS111	electrostatic stabiliser
E	LYS192	electrostatic stabiliser
E	LYS195	electrostatic stabiliser

site_id	MCSA6
Number of Residues	3
Details	M-CSA 481

Chain	Residue	Details
F	LYS111	electrostatic stabiliser
F	LYS192	electrostatic stabiliser
F	LYS195	electrostatic stabiliser

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