6HL7

Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum with mutated active site (R109A/K138A) and N-carbamoyl-L-phosphate bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004070	molecular_function	aspartate carbamoyltransferase activity
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	0016020	cellular_component	membrane
A	0016597	molecular_function	amino acid binding
A	0016740	molecular_function	transferase activity
A	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
A	0044205	biological_process	'de novo' UMP biosynthetic process
B	0004070	molecular_function	aspartate carbamoyltransferase activity
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	0016020	cellular_component	membrane
B	0016597	molecular_function	amino acid binding
B	0016740	molecular_function	transferase activity
B	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
B	0044205	biological_process	'de novo' UMP biosynthetic process
C	0004070	molecular_function	aspartate carbamoyltransferase activity
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	0016020	cellular_component	membrane
C	0016597	molecular_function	amino acid binding
C	0016740	molecular_function	transferase activity
C	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
C	0044205	biological_process	'de novo' UMP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue CP A 401

Chain	Residue
A	SER107
A	THR108
A	ALA109
A	THR110
A	ARG159
A	HIS187
A	PRO333
A	LEU334
A	PRO335

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site_id	AC2
Number of Residues	9
Details	binding site for residue CP C 401

Chain	Residue
C	SER107
C	THR110
C	ARG159
C	HIS187
C	ARG226
C	ARG295
C	LEU334
C	PRO335
C	HOH506

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Functional Information from PROSITE/UniProt

site_id	PS00181
Number of Residues	17
Details	GLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPIinag.NGTGeHptqS

Chain	Residue	Details
A	LYS175-SER191

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