Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6XHS

Crystal structure of S. aureus TarI in complex with CTP (space group P1211)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0008299	biological_process	isoprenoid biosynthetic process
A	0016779	molecular_function	nucleotidyltransferase activity
A	0019350	biological_process	teichoic acid biosynthetic process
A	0047349	molecular_function	D-ribitol-5-phosphate cytidylyltransferase activity
A	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
A	0070567	molecular_function	cytidylyltransferase activity
A	0071555	biological_process	cell wall organization
A	1902012	biological_process	poly(ribitol phosphate) teichoic acid biosynthetic process
B	0003824	molecular_function	catalytic activity
B	0008299	biological_process	isoprenoid biosynthetic process
B	0016779	molecular_function	nucleotidyltransferase activity
B	0019350	biological_process	teichoic acid biosynthetic process
B	0047349	molecular_function	D-ribitol-5-phosphate cytidylyltransferase activity
B	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
B	0070567	molecular_function	cytidylyltransferase activity
B	0071555	biological_process	cell wall organization
B	1902012	biological_process	poly(ribitol phosphate) teichoic acid biosynthetic process
C	0003824	molecular_function	catalytic activity
C	0008299	biological_process	isoprenoid biosynthetic process
C	0016779	molecular_function	nucleotidyltransferase activity
C	0019350	biological_process	teichoic acid biosynthetic process
C	0047349	molecular_function	D-ribitol-5-phosphate cytidylyltransferase activity
C	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
C	0070567	molecular_function	cytidylyltransferase activity
C	0071555	biological_process	cell wall organization
C	1902012	biological_process	poly(ribitol phosphate) teichoic acid biosynthetic process
D	0003824	molecular_function	catalytic activity
D	0008299	biological_process	isoprenoid biosynthetic process
D	0016779	molecular_function	nucleotidyltransferase activity
D	0019350	biological_process	teichoic acid biosynthetic process
D	0047349	molecular_function	D-ribitol-5-phosphate cytidylyltransferase activity
D	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
D	0070567	molecular_function	cytidylyltransferase activity
D	0071555	biological_process	cell wall organization
D	1902012	biological_process	poly(ribitol phosphate) teichoic acid biosynthetic process
E	0003824	molecular_function	catalytic activity
E	0008299	biological_process	isoprenoid biosynthetic process
E	0016779	molecular_function	nucleotidyltransferase activity
E	0019350	biological_process	teichoic acid biosynthetic process
E	0047349	molecular_function	D-ribitol-5-phosphate cytidylyltransferase activity
E	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
E	0070567	molecular_function	cytidylyltransferase activity
E	0071555	biological_process	cell wall organization
E	1902012	biological_process	poly(ribitol phosphate) teichoic acid biosynthetic process
F	0003824	molecular_function	catalytic activity
F	0008299	biological_process	isoprenoid biosynthetic process
F	0016779	molecular_function	nucleotidyltransferase activity
F	0019350	biological_process	teichoic acid biosynthetic process
F	0047349	molecular_function	D-ribitol-5-phosphate cytidylyltransferase activity
F	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
F	0070567	molecular_function	cytidylyltransferase activity
F	0071555	biological_process	cell wall organization
F	1902012	biological_process	poly(ribitol phosphate) teichoic acid biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue CTP B 301

Chain	Residue
B	LEU7
B	ASP111
B	ALA112
B	VAL113
B	LYS217
B	THR219
B	ALA8
B	GLY9
B	GLY10
B	GLY81
B	SER82
B	ASP83
B	ARG84
B	THR87

site_id	AC2
Number of Residues	4
Details	binding site for residue SCN C 301

Chain	Residue
C	GLY10
C	ILE11
C	GLN23
C	VAL113

site_id	AC3
Number of Residues	19
Details	binding site for residue CTP E 301

Chain	Residue
E	LEU7
E	ALA8
E	GLY9
E	GLY10
E	GLY12
E	SER13
E	ARG14
E	LYS22
E	GLY81
E	SER82
E	ASP83
E	ARG84
E	THR87
E	ASP111
E	ALA112
E	VAL113
E	LYS217
E	THR219
E	MG302

site_id	AC4
Number of Residues	4
Details	binding site for residue MG E 302

Chain	Residue
E	CTP301
E	HOH401
E	HOH402
E	HOH403

site_id	AC5
Number of Residues	6
Details	binding site for residue SCN F 301

Chain	Residue
F	LEU7
F	GLY10
F	GLN23
F	ASP111
F	ALA112
F	VAL113

Functional Information from PROSITE/UniProt

site_id	PS01295
Number of Residues	8
Details	ISPD 4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature. IVTHDAVR

Chain	Residue	Details
A	ILE107-ARG114

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_02068

Chain	Residue	Details
A	LEU7
A	GLY81
B	LEU7
B	GLY81
C	LEU7
C	GLY81
D	LEU7
D	GLY81
E	LEU7
E	GLY81
F	LEU7
F	GLY81

site_id	SWS_FT_FI2
Number of Residues	12
Details	SITE: Transition state stabilizer => ECO:0000255\|HAMAP-Rule:MF_02068

Chain	Residue	Details
B	ARG14
B	LYS22
C	ARG14
C	LYS22
D	ARG14
D	LYS22
E	ARG14
E	LYS22
F	ARG14
F	LYS22
A	ARG14
A	LYS22

site_id	SWS_FT_FI3
Number of Residues	12
Details	SITE: Positions ribitol 5-phosphate for the nucleophilic attack => ECO:0000255\|HAMAP-Rule:MF_02068

Chain	Residue	Details
B	ARG160
B	LYS217
C	ARG160
C	LYS217
D	ARG160
D	LYS217
E	ARG160
E	LYS217
F	ARG160
F	LYS217
A	ARG160
A	LYS217

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