Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5U6R

E. coli CTP synthase CC mutant filament (product-bound)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0003883	molecular_function	CTP synthase activity
A	0004359	molecular_function	glutaminase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006221	biological_process	pyrimidine nucleotide biosynthetic process
A	0006241	biological_process	CTP biosynthetic process
A	0016874	molecular_function	ligase activity
A	0019856	biological_process	pyrimidine nucleobase biosynthetic process
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0044210	biological_process	'de novo' CTP biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0051289	biological_process	protein homotetramerization
A	0097268	cellular_component	cytoophidium
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003883	molecular_function	CTP synthase activity
B	0004359	molecular_function	glutaminase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006221	biological_process	pyrimidine nucleotide biosynthetic process
B	0006241	biological_process	CTP biosynthetic process
B	0016874	molecular_function	ligase activity
B	0019856	biological_process	pyrimidine nucleobase biosynthetic process
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0044210	biological_process	'de novo' CTP biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0051289	biological_process	protein homotetramerization
B	0097268	cellular_component	cytoophidium
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003883	molecular_function	CTP synthase activity
C	0004359	molecular_function	glutaminase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006221	biological_process	pyrimidine nucleotide biosynthetic process
C	0006241	biological_process	CTP biosynthetic process
C	0016874	molecular_function	ligase activity
C	0019856	biological_process	pyrimidine nucleobase biosynthetic process
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0044210	biological_process	'de novo' CTP biosynthetic process
C	0046872	molecular_function	metal ion binding
C	0051289	biological_process	protein homotetramerization
C	0097268	cellular_component	cytoophidium
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003883	molecular_function	CTP synthase activity
D	0004359	molecular_function	glutaminase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006221	biological_process	pyrimidine nucleotide biosynthetic process
D	0006241	biological_process	CTP biosynthetic process
D	0016874	molecular_function	ligase activity
D	0019856	biological_process	pyrimidine nucleobase biosynthetic process
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0044210	biological_process	'de novo' CTP biosynthetic process
D	0046872	molecular_function	metal ion binding
D	0051289	biological_process	protein homotetramerization
D	0097268	cellular_component	cytoophidium

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue CTP A 601

Chain	Residue
A	ASP147
A	ILE148
A	GLU149
B	GLN114
B	VAL115
B	ILE116
C	THR188
C	LYS189
C	LYS196

site_id	AC2
Number of Residues	9
Details	binding site for residue ADP A 602

Chain	Residue
A	LEU16
A	GLY17
A	LYS18
A	ILE20
A	ASP72
A	ARG211
A	LYS239
A	ASP240
A	VAL241

site_id	AC3
Number of Residues	8
Details	binding site for residue CTP B 601

Chain	Residue
A	GLN114
B	SER14
B	ASP147
B	ILE148
B	GLU149
D	THR188
D	LYS189
D	LYS196

site_id	AC4
Number of Residues	9
Details	binding site for residue ADP B 602

Chain	Residue
B	LEU16
B	GLY17
B	LYS18
B	GLY19
B	ILE20
B	ARG211
B	LYS239
B	ASP240
B	VAL241

site_id	AC5
Number of Residues	8
Details	binding site for residue CTP C 601

Chain	Residue
A	THR188
A	LYS189
A	LYS196
C	SER14
C	ASP147
C	ILE148
C	GLU149
D	GLN114

site_id	AC6
Number of Residues	10
Details	binding site for residue ADP C 602

Chain	Residue
C	LEU16
C	GLY17
C	LYS18
C	GLY19
C	ILE20
C	ASP72
C	ARG211
C	LYS239
C	ASP240
C	VAL241

site_id	AC7
Number of Residues	8
Details	binding site for residue CTP D 601

Chain	Residue
B	THR188
B	LYS189
B	LYS196
C	ILE116
D	SER14
D	ASP147
D	ILE148
D	GLU149

site_id	AC8
Number of Residues	9
Details	binding site for residue ADP D 602

Chain	Residue
D	LEU16
D	GLY17
D	LYS18
D	GLY19
D	ILE20
D	ARG211
D	LYS239
D	ASP240
D	VAL241

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1060
Details	Region: {"description":"Amidoligase domain","evidences":[{"source":"HAMAP-Rule","id":"MF_01227","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"source":"PubMed","id":"11336655","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15157079","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Active site: {"evidences":[{"source":"PubMed","id":"15157079","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16216072","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16216072","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2AD5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16216072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AD5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01227","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1056
Details	Region: {"description":"Amidoligase domain","evidences":[{"source":"PubMed","id":"15157079","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)