Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6XHS

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008299biological_processisoprenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0019350biological_processteichoic acid biosynthetic process
A0047349molecular_functionD-ribitol-5-phosphate cytidylyltransferase activity
A0050518molecular_function2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
A0070567molecular_functioncytidylyltransferase activity
A0071555biological_processcell wall organization
A1902012biological_processpoly(ribitol phosphate) teichoic acid biosynthetic process
B0003824molecular_functioncatalytic activity
B0008299biological_processisoprenoid biosynthetic process
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0019350biological_processteichoic acid biosynthetic process
B0047349molecular_functionD-ribitol-5-phosphate cytidylyltransferase activity
B0050518molecular_function2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
B0070567molecular_functioncytidylyltransferase activity
B0071555biological_processcell wall organization
B1902012biological_processpoly(ribitol phosphate) teichoic acid biosynthetic process
C0003824molecular_functioncatalytic activity
C0008299biological_processisoprenoid biosynthetic process
C0016740molecular_functiontransferase activity
C0016779molecular_functionnucleotidyltransferase activity
C0019350biological_processteichoic acid biosynthetic process
C0047349molecular_functionD-ribitol-5-phosphate cytidylyltransferase activity
C0050518molecular_function2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
C0070567molecular_functioncytidylyltransferase activity
C0071555biological_processcell wall organization
C1902012biological_processpoly(ribitol phosphate) teichoic acid biosynthetic process
D0003824molecular_functioncatalytic activity
D0008299biological_processisoprenoid biosynthetic process
D0016740molecular_functiontransferase activity
D0016779molecular_functionnucleotidyltransferase activity
D0019350biological_processteichoic acid biosynthetic process
D0047349molecular_functionD-ribitol-5-phosphate cytidylyltransferase activity
D0050518molecular_function2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
D0070567molecular_functioncytidylyltransferase activity
D0071555biological_processcell wall organization
D1902012biological_processpoly(ribitol phosphate) teichoic acid biosynthetic process
E0003824molecular_functioncatalytic activity
E0008299biological_processisoprenoid biosynthetic process
E0016740molecular_functiontransferase activity
E0016779molecular_functionnucleotidyltransferase activity
E0019350biological_processteichoic acid biosynthetic process
E0047349molecular_functionD-ribitol-5-phosphate cytidylyltransferase activity
E0050518molecular_function2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
E0070567molecular_functioncytidylyltransferase activity
E0071555biological_processcell wall organization
E1902012biological_processpoly(ribitol phosphate) teichoic acid biosynthetic process
F0003824molecular_functioncatalytic activity
F0008299biological_processisoprenoid biosynthetic process
F0016740molecular_functiontransferase activity
F0016779molecular_functionnucleotidyltransferase activity
F0019350biological_processteichoic acid biosynthetic process
F0047349molecular_functionD-ribitol-5-phosphate cytidylyltransferase activity
F0050518molecular_function2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
F0070567molecular_functioncytidylyltransferase activity
F0071555biological_processcell wall organization
F1902012biological_processpoly(ribitol phosphate) teichoic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue CTP B 301
ChainResidue
BLEU7
BASP111
BALA112
BVAL113
BLYS217
BTHR219
BALA8
BGLY9
BGLY10
BGLY81
BSER82
BASP83
BARG84
BTHR87

site_idAC2
Number of Residues4
Detailsbinding site for residue SCN C 301
ChainResidue
CGLY10
CILE11
CGLN23
CVAL113

site_idAC3
Number of Residues19
Detailsbinding site for residue CTP E 301
ChainResidue
ELEU7
EALA8
EGLY9
EGLY10
EGLY12
ESER13
EARG14
ELYS22
EGLY81
ESER82
EASP83
EARG84
ETHR87
EASP111
EALA112
EVAL113
ELYS217
ETHR219
EMG302

site_idAC4
Number of Residues4
Detailsbinding site for residue MG E 302
ChainResidue
ECTP301
EHOH401
EHOH402
EHOH403

site_idAC5
Number of Residues6
Detailsbinding site for residue SCN F 301
ChainResidue
FLEU7
FGLY10
FGLN23
FASP111
FALA112
FVAL113

Functional Information from PROSITE/UniProt
site_idPS01295
Number of Residues8
DetailsISPD 4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature. IVTHDAVR
ChainResidueDetails
AILE107-ARG114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues54
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02068","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues11
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_02068","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsSite: {"description":"Positions ribitol 5-phosphate for the nucleophilic attack","evidences":[{"source":"HAMAP-Rule","id":"MF_02068","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

PDB statisticsPDBj update infoContact PDBjnumon