Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2ASH

Crystal structure of Queuine tRNA-ribosyltransferase (EC 2.4.2.29) (tRNA-guanine (tm1561) from THERMOTOGA MARITIMA at 1.90 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002099	biological_process	tRNA wobble guanine modification
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006400	biological_process	tRNA modification
A	0008033	biological_process	tRNA processing
A	0008479	molecular_function	tRNA-guanosine(34) queuine transglycosylase activity
A	0008616	biological_process	tRNA queuosine(34) biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0046872	molecular_function	metal ion binding
B	0002099	biological_process	tRNA wobble guanine modification
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006400	biological_process	tRNA modification
B	0008033	biological_process	tRNA processing
B	0008479	molecular_function	tRNA-guanosine(34) queuine transglycosylase activity
B	0008616	biological_process	tRNA queuosine(34) biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0046872	molecular_function	metal ion binding
C	0002099	biological_process	tRNA wobble guanine modification
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006400	biological_process	tRNA modification
C	0008033	biological_process	tRNA processing
C	0008479	molecular_function	tRNA-guanosine(34) queuine transglycosylase activity
C	0008616	biological_process	tRNA queuosine(34) biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0046872	molecular_function	metal ion binding
D	0002099	biological_process	tRNA wobble guanine modification
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006400	biological_process	tRNA modification
D	0008033	biological_process	tRNA processing
D	0008479	molecular_function	tRNA-guanosine(34) queuine transglycosylase activity
D	0008616	biological_process	tRNA queuosine(34) biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 400

Chain	Residue
A	CYS299
A	CYS301
A	CYS304
A	HIS330

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 400

Chain	Residue
B	CYS299
B	CYS301
B	CYS304
B	HIS330

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 400

Chain	Residue
C	CYS301
C	CYS304
C	HIS330
C	CYS299

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 400

Chain	Residue
D	CYS299
D	CYS301
D	CYS304
D	HIS330

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 401

Chain	Residue
C	HOH455
D	VAL321
D	HOH510

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 401

Chain	Residue
A	VAL321
A	HOH421
A	HOH515
B	HOH529

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 401

Chain	Residue
A	ARG309
C	TYR287
C	ARG290
C	SER291
C	HOH495

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL A 402

Chain	Residue
A	TYR287
A	LYS289
A	ARG290
A	SER291
A	HOH553
C	ARG309
C	HOH412

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL C 402

Chain	Residue
C	ARG270
C	HOH433

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 403

Chain	Residue
C	CYS304
C	LYS305
C	PHE307

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 402

Chain	Residue
C	PRO65
D	LYS289
D	SER310
D	HIS313
D	HIS314
D	HOH449

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 404

Chain	Residue
C	SER213
C	ILE214
C	GLY215
C	GLU216
C	ARG218
C	THR221

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 405

Chain	Residue
C	GLU320
C	VAL321
C	LEU322
C	HOH436
C	HOH483
D	LYS39
D	LEU40

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 401

Chain	Residue
A	LYS39
A	LEU40
B	GLU320
B	VAL321
B	LEU322
B	HOH496
B	HOH572

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 406

Chain	Residue
C	CYS144
C	GLY210
C	GLY211
C	LEU212
C	ILE214
C	MET241
C	HOH488
C	HOH524

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 403

Chain	Residue
A	GLU347
C	CYS299
C	GLY300
C	ASN333
C	HOH462
C	HOH529

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 404

Chain	Residue
A	CYS144
A	GLY210
A	GLY211
A	LEU212
A	ILE214
A	MET241
A	HOH483
A	HOH552

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 405

Chain	Residue
A	CYS304
A	LYS305
A	ASN306
A	PHE307

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 403

Chain	Residue
D	HOH562
D	CYS144
D	GLY210
D	GLY211
D	LEU212
D	ILE214
D	MET241
D	HOH473

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Region: {"description":"RNA binding","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Region: {"description":"RNA binding; important for wobble base 34 recognition","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of queuine tRNA-ribosyltransferase (EC 2.4.2.29) (tRNA-guanine (tm1561) from Thermotoga maritima at 1.90 A resolution.","authoringGroup":["Joint Center for Structural Genomics (JCSG)"]}}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP89

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

Chain	Residue	Details
B	ASP89

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

Chain	Residue	Details
C	ASP89

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

Chain	Residue	Details
D	ASP89

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