Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6KJ9

E. coli ATCase catalytic subunit mutant - G128/130A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004070	molecular_function	aspartate carbamoyltransferase activity
A	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
A	0006221	biological_process	pyrimidine nucleotide biosynthetic process
A	0006520	biological_process	amino acid metabolic process
A	0006541	biological_process	glutamine metabolic process
A	0016597	molecular_function	amino acid binding
A	0016740	molecular_function	transferase activity
A	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
A	0042802	molecular_function	identical protein binding
A	0044205	biological_process	'de novo' UMP biosynthetic process
A	0070207	biological_process	protein homotrimerization
B	0004070	molecular_function	aspartate carbamoyltransferase activity
B	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
B	0006221	biological_process	pyrimidine nucleotide biosynthetic process
B	0006520	biological_process	amino acid metabolic process
B	0006541	biological_process	glutamine metabolic process
B	0016597	molecular_function	amino acid binding
B	0016740	molecular_function	transferase activity
B	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
B	0042802	molecular_function	identical protein binding
B	0044205	biological_process	'de novo' UMP biosynthetic process
B	0070207	biological_process	protein homotrimerization
C	0004070	molecular_function	aspartate carbamoyltransferase activity
C	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
C	0006221	biological_process	pyrimidine nucleotide biosynthetic process
C	0006520	biological_process	amino acid metabolic process
C	0006541	biological_process	glutamine metabolic process
C	0016597	molecular_function	amino acid binding
C	0016740	molecular_function	transferase activity
C	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
C	0042802	molecular_function	identical protein binding
C	0044205	biological_process	'de novo' UMP biosynthetic process
C	0070207	biological_process	protein homotrimerization
D	0004070	molecular_function	aspartate carbamoyltransferase activity
D	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
D	0006221	biological_process	pyrimidine nucleotide biosynthetic process
D	0006520	biological_process	amino acid metabolic process
D	0006541	biological_process	glutamine metabolic process
D	0016597	molecular_function	amino acid binding
D	0016740	molecular_function	transferase activity
D	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
D	0042802	molecular_function	identical protein binding
D	0044205	biological_process	'de novo' UMP biosynthetic process
D	0070207	biological_process	protein homotrimerization
E	0004070	molecular_function	aspartate carbamoyltransferase activity
E	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
E	0006221	biological_process	pyrimidine nucleotide biosynthetic process
E	0006520	biological_process	amino acid metabolic process
E	0006541	biological_process	glutamine metabolic process
E	0016597	molecular_function	amino acid binding
E	0016740	molecular_function	transferase activity
E	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
E	0042802	molecular_function	identical protein binding
E	0044205	biological_process	'de novo' UMP biosynthetic process
E	0070207	biological_process	protein homotrimerization
F	0004070	molecular_function	aspartate carbamoyltransferase activity
F	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
F	0006221	biological_process	pyrimidine nucleotide biosynthetic process
F	0006520	biological_process	amino acid metabolic process
F	0006541	biological_process	glutamine metabolic process
F	0016597	molecular_function	amino acid binding
F	0016740	molecular_function	transferase activity
F	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
F	0042802	molecular_function	identical protein binding
F	0044205	biological_process	'de novo' UMP biosynthetic process
F	0070207	biological_process	protein homotrimerization

Functional Information from PROSITE/UniProt

site_id	PS00097
Number of Residues	8
Details	CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT

Chain	Residue	Details
A	PHE48-THR55

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3380787","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3380787","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 405

Chain	Residue	Details
A	ARG54	electrostatic stabiliser
A	THR55	electrostatic stabiliser, increase electrophilicity
A	LYS84	proton shuttle (general acid/base)
A	ARG105	electrostatic stabiliser, increase electrophilicity
A	HIS134	electrostatic stabiliser, increase electrophilicity

site_id	MCSA2
Number of Residues	4
Details	M-CSA 405

Chain	Residue	Details
B	ARG54	electrostatic stabiliser
B	THR55	electrostatic stabiliser, increase electrophilicity
B	ARG105	electrostatic stabiliser, increase electrophilicity
B	HIS134	electrostatic stabiliser, increase electrophilicity

site_id	MCSA3
Number of Residues	4
Details	M-CSA 405

Chain	Residue	Details
C	ARG54	electrostatic stabiliser
C	THR55	electrostatic stabiliser, increase electrophilicity
C	ARG105	electrostatic stabiliser, increase electrophilicity
C	HIS134	electrostatic stabiliser, increase electrophilicity

site_id	MCSA4
Number of Residues	4
Details	M-CSA 405

Chain	Residue	Details
D	ARG54	electrostatic stabiliser
D	THR55	electrostatic stabiliser, increase electrophilicity
D	ARG105	electrostatic stabiliser, increase electrophilicity
D	HIS134	electrostatic stabiliser, increase electrophilicity

site_id	MCSA5
Number of Residues	4
Details	M-CSA 405

Chain	Residue	Details
E	ARG54	electrostatic stabiliser
E	THR55	electrostatic stabiliser, increase electrophilicity
E	ARG105	electrostatic stabiliser, increase electrophilicity
E	HIS134	electrostatic stabiliser, increase electrophilicity

site_id	MCSA6
Number of Residues	4
Details	M-CSA 405

Chain	Residue	Details
F	ARG54	electrostatic stabiliser
F	THR55	electrostatic stabiliser, increase electrophilicity
F	ARG105	electrostatic stabiliser, increase electrophilicity
F	HIS134	electrostatic stabiliser, increase electrophilicity

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)