Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6XHR

Crystal structure of S. aureus TarI (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	0016740	molecular_function	transferase activity
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	0016740	molecular_function	transferase activity
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	0016740	molecular_function	transferase activity
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	0016740	molecular_function	transferase activity
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	0016740	molecular_function	transferase activity
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	0016740	molecular_function	transferase activity
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	7
Details	binding site for residue SCN A 301

Chain	Residue
A	LEU7
A	GLY10
A	GLN23
A	ASP111
A	ALA112
A	VAL113
A	HOH445

site_id	AC2
Number of Residues	3
Details	binding site for residue SCN A 302

Chain	Residue
D	LYS123
A	PRO21
A	LYS22

site_id	AC3
Number of Residues	8
Details	binding site for residue SCN C 301

Chain	Residue
C	LEU7
C	ALA8
C	GLY10
C	GLN23
C	ASP111
C	ALA112
C	VAL113
C	HOH404

site_id	AC4
Number of Residues	3
Details	binding site for residue SCN C 302

Chain	Residue
B	LYS123
C	PRO21
C	LYS22

site_id	AC5
Number of Residues	5
Details	binding site for residue SCN D 301

Chain	Residue
D	LEU7
D	GLY10
D	GLN23
D	ASP111
D	ALA112

site_id	AC6
Number of Residues	2
Details	binding site for residue SCN D 302

Chain	Residue
D	PRO21
D	LYS22

site_id	AC7
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

site_id	AC8
Number of Residues	3
Details	binding site for residue SCN F 302

Chain	Residue
F	PRO21
F	LYS22
F	HOH418

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
E	GLY81
F	LEU7
F	GLY81
A	GLY81
B	LEU7
B	GLY81
C	LEU7
C	GLY81
D	LEU7
D	GLY81
E	LEU7

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

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

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
A	ARG160
E	LYS217
F	ARG160
F	LYS217
A	LYS217
B	ARG160
B	LYS217
C	ARG160
C	LYS217
D	ARG160
D	LYS217
E	ARG160

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