5Z0A

ST0452(Y97N)-GlcNAc binding form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
A	0003983	molecular_function	UTP:glucose-1-phosphate uridylyltransferase activity
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0008879	molecular_function	glucose-1-phosphate thymidylyltransferase activity
A	0009058	biological_process	biosynthetic process
A	0016779	molecular_function	nucleotidyltransferase activity
A	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
A	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase activity
B	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
B	0003983	molecular_function	UTP:glucose-1-phosphate uridylyltransferase activity
B	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
B	0008879	molecular_function	glucose-1-phosphate thymidylyltransferase activity
B	0009058	biological_process	biosynthetic process
B	0016779	molecular_function	nucleotidyltransferase activity
B	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
B	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase activity
C	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
C	0003983	molecular_function	UTP:glucose-1-phosphate uridylyltransferase activity
C	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
C	0008879	molecular_function	glucose-1-phosphate thymidylyltransferase activity
C	0009058	biological_process	biosynthetic process
C	0016779	molecular_function	nucleotidyltransferase activity
C	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
C	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase activity
D	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
D	0003983	molecular_function	UTP:glucose-1-phosphate uridylyltransferase activity
D	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
D	0008879	molecular_function	glucose-1-phosphate thymidylyltransferase activity
D	0009058	biological_process	biosynthetic process
D	0016779	molecular_function	nucleotidyltransferase activity
D	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
D	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase activity
E	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
E	0003983	molecular_function	UTP:glucose-1-phosphate uridylyltransferase activity
E	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
E	0008879	molecular_function	glucose-1-phosphate thymidylyltransferase activity
E	0009058	biological_process	biosynthetic process
E	0016779	molecular_function	nucleotidyltransferase activity
E	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
E	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase activity
F	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
F	0003983	molecular_function	UTP:glucose-1-phosphate uridylyltransferase activity
F	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
F	0008879	molecular_function	glucose-1-phosphate thymidylyltransferase activity
F	0009058	biological_process	biosynthetic process
F	0016779	molecular_function	nucleotidyltransferase activity
F	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
F	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	876
Details	Region: {"description":"Nucleotidylyltransferase","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	42
Details	Binding 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."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30291121","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5Z0A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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