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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5Z09

ST0452(Y97N)-UTP binding form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
A0052630molecular_functionUDP-N-acetylgalactosamine diphosphorylase activity
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
B0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
B0052630molecular_functionUDP-N-acetylgalactosamine diphosphorylase activity
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
C0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
C0006048biological_processUDP-N-acetylglucosamine biosynthetic process
C0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
C0009058biological_processbiosynthetic process
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0016779molecular_functionnucleotidyltransferase activity
C0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
C0052630molecular_functionUDP-N-acetylgalactosamine diphosphorylase activity
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
D0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
D0006048biological_processUDP-N-acetylglucosamine biosynthetic process
D0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
D0009058biological_processbiosynthetic process
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
D0016779molecular_functionnucleotidyltransferase activity
D0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
D0052630molecular_functionUDP-N-acetylgalactosamine diphosphorylase activity
E0000166molecular_functionnucleotide binding
E0003824molecular_functioncatalytic activity
E0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
E0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
E0006048biological_processUDP-N-acetylglucosamine biosynthetic process
E0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
E0009058biological_processbiosynthetic process
E0016740molecular_functiontransferase activity
E0016746molecular_functionacyltransferase activity
E0016779molecular_functionnucleotidyltransferase activity
E0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
E0052630molecular_functionUDP-N-acetylgalactosamine diphosphorylase activity
F0000166molecular_functionnucleotide binding
F0003824molecular_functioncatalytic activity
F0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
F0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
F0006048biological_processUDP-N-acetylglucosamine biosynthetic process
F0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
F0009058biological_processbiosynthetic process
F0016740molecular_functiontransferase activity
F0016746molecular_functionacyltransferase activity
F0016779molecular_functionnucleotidyltransferase activity
F0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
F0052630molecular_functionUDP-N-acetylgalactosamine diphosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue UTP A 501
ChainResidue
ALEU6
AGLN73
AGLY79
ATHR80
AGLY98
AASP99
AARG179
AALA7
AALA8
AGLY9
ASER10
AGLY11
AGLU12
AARG13
ALYS23
site_idAC2
Number of Residues15
Detailsbinding site for residue UTP B 501
ChainResidue
BLEU6
BALA7
BALA8
BGLY9
BGLY11
BARG13
BLYS23
BGLN73
BGLY79
BTHR80
BALA83
BASN97
BGLY98
BASP99
BARG179
site_idAC3
Number of Residues14
Detailsbinding site for residue UTP C 501
ChainResidue
CLEU6
CALA7
CALA8
CGLY9
CSER10
CGLY11
CGLU12
CARG13
CLYS23
CGLN73
CGLY79
CTHR80
CGLY98
CASP99
site_idAC4
Number of Residues14
Detailsbinding site for residue UTP D 501
ChainResidue
DLEU6
DALA7
DALA8
DGLY9
DSER10
DGLY11
DGLU12
DARG13
DGLN73
DLYS78
DGLY79
DTHR80
DGLY98
DASP99
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues876
DetailsRegion: {"description":"Nucleotidylyltransferase","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues990
DetailsRegion: {"description":"Acetyltransferase","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues41
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30291121","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of glucose-1-phosphate thymidylyltransferase from Sulfolobus tokodaii.","authors":["Rajakannan V.","Yamane T."]}}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues29
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30291121","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5Z0A","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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