Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6XHT

Crystal structure of S. aureus TarI in complex with CDP-ribitol (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	HOH543

site_id	AC2
Number of Residues	5
Details	binding site for residue SCN A 302

Chain	Residue
A	LYS22
A	HOH453
D	LYS123
A	LEU20
A	PRO21

site_id	AC3
Number of Residues	30
Details	binding site for residue V2V B 301

Chain	Residue
A	ASP143
A	THR144
A	ARG160
B	LEU7
B	ALA8
B	GLY9
B	GLY10
B	GLY81
B	SER82
B	ASP83
B	ARG84
B	THR87
B	ASP111
B	ALA112
B	VAL113
B	ARG114
B	GLY166
B	GLN167
B	GLN170
B	SER193
B	LYS217
B	THR219
B	HOH422
B	HOH435
B	HOH448
B	HOH463
B	HOH503
B	HOH504
B	HOH533
B	HOH537

site_id	AC4
Number of Residues	4
Details	binding site for residue SCN B 302

Chain	Residue
B	PHE24
B	HIS60
B	THR64
B	HOH489

site_id	AC5
Number of Residues	3
Details	binding site for residue SCN B 303

Chain	Residue
B	LYS48
B	HIS94
B	THR98

site_id	AC6
Number of Residues	6
Details	binding site for residue SCN C 301

Chain	Residue
C	LEU7
C	GLY10
C	GLN23
C	ALA112
C	VAL113
C	HOH475

site_id	AC7
Number of Residues	2
Details	binding site for residue SCN C 302

Chain	Residue
C	PRO21
C	LYS22

site_id	AC8
Number of Residues	7
Details	binding site for residue SCN D 301

Chain	Residue
D	LEU7
D	GLY10
D	GLN23
D	ASP111
D	ALA112
D	VAL113
D	HOH479

site_id	AC9
Number of Residues	2
Details	binding site for residue SCN D 302

Chain	Residue
D	PRO21
D	LYS22

site_id	AD1
Number of Residues	29
Details	binding site for residue V2V E 301

Chain	Residue
E	LEU7
E	ALA8
E	GLY9
E	GLY10
E	GLY81
E	SER82
E	ASP83
E	ARG84
E	THR87
E	ASP111
E	ALA112
E	VAL113
E	ARG114
E	GLY166
E	GLN167
E	GLN170
E	SER193
E	LYS217
E	HOH410
E	HOH415
E	HOH433
E	HOH435
E	HOH449
E	HOH456
E	HOH458
E	HOH486
F	ASP143
F	THR144
F	ARG160

site_id	AD2
Number of Residues	5
Details	binding site for residue SCN E 302

Chain	Residue
E	HOH507
E	PHE24
E	PRO31
E	HIS60
E	THR64

site_id	AD3
Number of Residues	7
Details	binding site for residue SCN F 301

Chain	Residue
F	LEU7
F	GLY10
F	GLN23
F	ASP111
F	ALA112
F	VAL113
F	HOH490

site_id	AD4
Number of Residues	3
Details	binding site for residue SCN F 302

Chain	Residue
F	PRO21
F	LYS22
F	HOH492

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	54
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02068","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	11
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_02068","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Site: {"description":"Positions ribitol 5-phosphate for the nucleophilic attack","evidences":[{"source":"HAMAP-Rule","id":"MF_02068","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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