Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5U03

Cryo-EM structure of the human CTP synthase filament

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002376	biological_process	immune system process
A	0003883	molecular_function	CTP synthase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006221	biological_process	pyrimidine nucleotide biosynthetic process
A	0006241	biological_process	CTP biosynthetic process
A	0006541	biological_process	glutamine metabolic process
A	0009410	biological_process	response to xenobiotic stimulus
A	0016020	cellular_component	membrane
A	0016874	molecular_function	ligase activity
A	0019856	biological_process	pyrimidine nucleobase biosynthetic process
A	0042098	biological_process	T cell proliferation
A	0042100	biological_process	B cell proliferation
A	0042802	molecular_function	identical protein binding
A	0044210	biological_process	'de novo' CTP biosynthetic process
A	0097268	cellular_component	cytoophidium
B	0002376	biological_process	immune system process
B	0003883	molecular_function	CTP synthase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006221	biological_process	pyrimidine nucleotide biosynthetic process
B	0006241	biological_process	CTP biosynthetic process
B	0006541	biological_process	glutamine metabolic process
B	0009410	biological_process	response to xenobiotic stimulus
B	0016020	cellular_component	membrane
B	0016874	molecular_function	ligase activity
B	0019856	biological_process	pyrimidine nucleobase biosynthetic process
B	0042098	biological_process	T cell proliferation
B	0042100	biological_process	B cell proliferation
B	0042802	molecular_function	identical protein binding
B	0044210	biological_process	'de novo' CTP biosynthetic process
B	0097268	cellular_component	cytoophidium
C	0002376	biological_process	immune system process
C	0003883	molecular_function	CTP synthase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006221	biological_process	pyrimidine nucleotide biosynthetic process
C	0006241	biological_process	CTP biosynthetic process
C	0006541	biological_process	glutamine metabolic process
C	0009410	biological_process	response to xenobiotic stimulus
C	0016020	cellular_component	membrane
C	0016874	molecular_function	ligase activity
C	0019856	biological_process	pyrimidine nucleobase biosynthetic process
C	0042098	biological_process	T cell proliferation
C	0042100	biological_process	B cell proliferation
C	0042802	molecular_function	identical protein binding
C	0044210	biological_process	'de novo' CTP biosynthetic process
C	0097268	cellular_component	cytoophidium
D	0002376	biological_process	immune system process
D	0003883	molecular_function	CTP synthase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006221	biological_process	pyrimidine nucleotide biosynthetic process
D	0006241	biological_process	CTP biosynthetic process
D	0006541	biological_process	glutamine metabolic process
D	0009410	biological_process	response to xenobiotic stimulus
D	0016020	cellular_component	membrane
D	0016874	molecular_function	ligase activity
D	0019856	biological_process	pyrimidine nucleobase biosynthetic process
D	0042098	biological_process	T cell proliferation
D	0042100	biological_process	B cell proliferation
D	0042802	molecular_function	identical protein binding
D	0044210	biological_process	'de novo' CTP biosynthetic process
D	0097268	cellular_component	cytoophidium

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue ATP A 601

Chain	Residue
A	GLY13
A	VAL247
A	ASP312
A	UTP602
A	ILE14
A	GLY15
A	LYS16
A	GLY17
A	ILE18
A	ASP70
A	GLU146
A	ARG217

site_id	AC2
Number of Residues	16
Details	binding site for residue UTP A 602

Chain	Residue
A	SER12
A	LYS38
A	ASP40
A	PRO41
A	TYR42
A	GLU146
A	GLY148
A	GLY149
A	GLU155
A	ATP601
B	LYS193
B	THR194
B	LYS195
B	GLN198
B	PHE233
C	GLN112

site_id	AC3
Number of Residues	12
Details	binding site for residue ATP B 601

Chain	Residue
B	GLY13
B	ILE14
B	GLY15
B	LYS16
B	GLY17
B	ILE18
B	ASP70
B	GLU146
B	ARG217
B	VAL247
B	ASP312
B	UTP602

site_id	AC4
Number of Residues	16
Details	binding site for residue UTP B 602

Chain	Residue
A	LYS193
A	THR194
A	LYS195
A	GLN198
A	PHE233
B	SER12
B	LYS38
B	ASP40
B	PRO41
B	TYR42
B	GLU146
B	GLY148
B	GLY149
B	GLU155
B	ATP601
D	GLN112

site_id	AC5
Number of Residues	12
Details	binding site for residue ATP C 601

Chain	Residue
C	GLY13
C	ILE14
C	GLY15
C	LYS16
C	GLY17
C	ILE18
C	ASP70
C	GLU146
C	ARG217
C	VAL247
C	ASP312
C	UTP602

site_id	AC6
Number of Residues	16
Details	binding site for residue UTP C 602

Chain	Residue
A	GLN112
C	SER12
C	LYS38
C	ASP40
C	PRO41
C	TYR42
C	GLU146
C	GLY148
C	GLY149
C	GLU155
C	ATP601
D	LYS193
D	THR194
D	LYS195
D	GLN198
D	PHE233

site_id	AC7
Number of Residues	12
Details	binding site for residue ATP D 601

Chain	Residue
D	GLY13
D	ILE14
D	GLY15
D	LYS16
D	GLY17
D	ILE18
D	ASP70
D	GLU146
D	ARG217
D	VAL247
D	ASP312
D	UTP602

site_id	AC8
Number of Residues	16
Details	binding site for residue UTP D 602

Chain	Residue
C	LYS195
C	GLN198
C	PHE233
D	SER12
D	LYS38
D	ASP40
D	PRO41
D	TYR42
D	GLU146
D	GLY148
D	GLY149
D	GLU155
D	ATP601
B	GLN112
C	LYS193
C	THR194

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: For GATase activity => ECO:0000250

Chain	Residue	Details
A	CYS399
D	CYS399
D	HIS526
D	GLU528
A	HIS526
A	GLU528
B	CYS399
B	HIS526
B	GLU528
C	CYS399
C	HIS526
C	GLU528

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS100
B	LYS100
C	LYS100
D	LYS100

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:21406692

Chain	Residue	Details
A	SER562
B	SER562
C	SER562
D	SER562

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER568
A	SER587
B	SER568
B	SER587
C	SER568
C	SER587
D	SER568
D	SER587

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332

Chain	Residue	Details
A	SER571
B	SER571
C	SER571
D	SER571

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:21406692

Chain	Residue	Details
A	SER573
B	SER573
C	SER573
D	SER573

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
A	SER574
B	SER574
C	SER574
D	SER574

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER575
B	SER575
C	SER575
D	SER575

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P70698

Chain	Residue	Details
A	SER578
B	SER578
C	SER578
D	SER578

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