6PK7

cryoEM structure of the product-bound human CTP synthase 2 filament

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0006220	biological_process	pyrimidine nucleotide 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	0016874	molecular_function	ligase activity
A	0019637	biological_process	organophosphate metabolic process
A	0019856	biological_process	pyrimidine nucleobase biosynthetic process
A	0042802	molecular_function	identical protein binding
A	0044210	biological_process	'de novo' CTP biosynthetic process
A	0097268	cellular_component	cytoophidium
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	0006220	biological_process	pyrimidine nucleotide 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	0016874	molecular_function	ligase activity
D	0019637	biological_process	organophosphate metabolic process
D	0019856	biological_process	pyrimidine nucleobase biosynthetic process
D	0042802	molecular_function	identical protein binding
D	0044210	biological_process	'de novo' CTP biosynthetic process
D	0097268	cellular_component	cytoophidium
E	0003883	molecular_function	CTP synthase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006220	biological_process	pyrimidine nucleotide metabolic process
E	0006221	biological_process	pyrimidine nucleotide biosynthetic process
E	0006241	biological_process	CTP biosynthetic process
E	0006541	biological_process	glutamine metabolic process
E	0016874	molecular_function	ligase activity
E	0019637	biological_process	organophosphate metabolic process
E	0019856	biological_process	pyrimidine nucleobase biosynthetic process
E	0042802	molecular_function	identical protein binding
E	0044210	biological_process	'de novo' CTP biosynthetic process
E	0097268	cellular_component	cytoophidium
F	0003883	molecular_function	CTP synthase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006220	biological_process	pyrimidine nucleotide metabolic process
F	0006221	biological_process	pyrimidine nucleotide biosynthetic process
F	0006241	biological_process	CTP biosynthetic process
F	0006541	biological_process	glutamine metabolic process
F	0016874	molecular_function	ligase activity
F	0019637	biological_process	organophosphate metabolic process
F	0019856	biological_process	pyrimidine nucleobase biosynthetic process
F	0042802	molecular_function	identical protein binding
F	0044210	biological_process	'de novo' CTP biosynthetic process
F	0097268	cellular_component	cytoophidium

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue ADP A 601

Chain	Residue
A	SER12
A	PHE77
A	GLY13
A	GLY15
A	LYS16
A	GLY17
A	ILE18
A	SER21
A	ASP70
A	ASN73

---

site_id	AC2
Number of Residues	14
Details	binding site for residue CTP A 602

Chain	Residue
A	SER12
A	THR150
A	ASP153
A	ILE154
A	GLU155
D	LYS193
D	THR194
D	LYS195
D	GLN198
D	LYS229
D	PHE233
E	GLN112
E	VAL113
E	VAL114

---

site_id	AC3
Number of Residues	10
Details	binding site for residue ADP D 601

Chain	Residue
D	SER12
D	GLY13
D	GLY15
D	LYS16
D	GLY17
D	ILE18
D	SER21
D	ASP70
D	ASN73
D	PHE77

---

site_id	AC4
Number of Residues	14
Details	binding site for residue CTP D 602

Chain	Residue
A	LYS193
A	THR194
A	LYS195
A	GLN198
A	LYS229
A	PHE233
D	SER12
D	THR150
D	ASP153
D	ILE154
D	GLU155
F	GLN112
F	VAL113
F	VAL114

---

site_id	AC5
Number of Residues	10
Details	binding site for residue ADP E 601

Chain	Residue
E	SER12
E	GLY13
E	GLY15
E	LYS16
E	GLY17
E	ILE18
E	SER21
E	ASP70
E	ASN73
E	PHE77

---

site_id	AC6
Number of Residues	14
Details	binding site for residue CTP E 602

Chain	Residue
A	GLN112
A	VAL113
A	VAL114
E	SER12
E	THR150
E	ASP153
E	ILE154
E	GLU155
F	LYS193
F	THR194
F	LYS195
F	GLN198
F	LYS229
F	PHE233

---

site_id	AC7
Number of Residues	10
Details	binding site for residue ADP F 601

Chain	Residue
F	SER12
F	GLY13
F	GLY15
F	LYS16
F	GLY17
F	ILE18
F	SER21
F	ASP70
F	ASN73
F	PHE77

---

site_id	AC8
Number of Residues	14
Details	binding site for residue CTP F 602

Chain	Residue
D	GLN112
D	VAL113
D	VAL114
E	LYS193
E	THR194
E	LYS195
E	GLN198
E	LYS229
E	PHE233
F	SER12
F	THR150
F	ASP153
F	ILE154
F	GLU155

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: For GATase activity => ECO:0000255|PROSITE-ProRule:PRU00605

Chain	Residue	Details
A	CYS399
F	CYS399
F	HIS526
F	GLU528
A	HIS526
A	GLU528
D	CYS399
D	HIS526
D	GLU528
E	CYS399
E	HIS526
E	GLU528

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER568
D	SER568
E	SER568
F	SER568

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER571
D	SER571
E	SER571
F	SER571

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER574
D	SER574
E	SER574
F	SER574

---