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1COZ

CTP:GLYCEROL-3-PHOSPHATE CYTIDYLYLTRANSFERASE FROM BACILLUS SUBTILIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0019350biological_processteichoic acid biosynthetic process
A0046872molecular_functionmetal ion binding
A0047348molecular_functionglycerol-3-phosphate cytidylyltransferase activity
A0071555biological_processcell wall organization
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0019350biological_processteichoic acid biosynthetic process
B0046872molecular_functionmetal ion binding
B0047348molecular_functionglycerol-3-phosphate cytidylyltransferase activity
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE CTP A 130
ChainResidue
ATHR9
AILE117
ASER118
ATHR119
ATHR120
AHOH1002
AHOH1042
AHOH1070
APHE10
AHIS14
AHIS17
ALYS46
AGLY92
AASP94
AARG113
ATHR114

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE CTP B 630
ChainResidue
BTHR509
BPHE510
BHIS514
BHIS517
BLYS546
BGLY592
BARG613
BTHR614
BILE617
BSER618
BTHR619
BTHR620
BHOH1003
BHOH1040
BHOH1050
BHOH1076
BHOH1080

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10508782, ECO:0000269|PubMed:14506262
ChainResidueDetails
ATHR9
AHIS14
ALYS46
AARG113
BTHR509
BHIS514
BLYS546
BARG613

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14506262
ChainResidueDetails
ALYS44
ALYS77
BLYS544
BLYS577

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 296
ChainResidueDetails
ALYS44attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
ALYS46attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 296
ChainResidueDetails
BLYS544attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
BLYS546attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-04-24

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