Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6JKT

Crystal structure of aspartate transcarbamoylase from Trypanosoma cruzi in complex with N-(PHOSPHONACETYL)-L-ASPARTIC ACID (PALA).

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004070	molecular_function	aspartate carbamoyltransferase activity
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	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	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	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	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	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
D	0004070	molecular_function	aspartate carbamoyltransferase activity
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	0016597	molecular_function	amino acid binding
D	0016740	molecular_function	transferase activity
D	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
D	0044205	biological_process	'de novo' UMP biosynthetic process
E	0004070	molecular_function	aspartate carbamoyltransferase activity
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	0016597	molecular_function	amino acid binding
E	0016740	molecular_function	transferase activity
E	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
E	0044205	biological_process	'de novo' UMP biosynthetic process
F	0004070	molecular_function	aspartate carbamoyltransferase activity
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	0016597	molecular_function	amino acid binding
F	0016740	molecular_function	transferase activity
F	0016743	molecular_function	carboxyl- or carbamoyltransferase activity
F	0044205	biological_process	'de novo' UMP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue PAL A 401

Chain	Residue
A	SER62
A	LEU288
A	HOH517
A	HOH529
A	HOH540
B	SER89
B	LYS92
A	SER63
A	ARG64
A	THR65
A	ARG113
A	HIS141
A	ARG174
A	ARG242
A	GLN244

site_id	AC2
Number of Residues	6
Details	binding site for residue GOL A 402

Chain	Residue
A	SER9
A	LEU10
A	GLN20
A	PHE21
A	ASP25
A	HOH542

site_id	AC3
Number of Residues	15
Details	binding site for residue PAL B 401

Chain	Residue
B	SER62
B	SER63
B	ARG64
B	THR65
B	ARG113
B	HIS141
B	ARG174
B	ARG242
B	GLN244
B	LEU288
B	HOH513
B	HOH515
B	HOH543
C	SER89
C	LYS92

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL B 402

Chain	Residue
B	SER9
B	GLN20
B	PHE21
B	ASP25
B	HOH507
B	HOH518

site_id	AC5
Number of Residues	14
Details	binding site for residue PAL C 401

Chain	Residue
A	SER89
A	LYS92
C	SER62
C	SER63
C	ARG64
C	THR65
C	ARG113
C	HIS141
C	ARG174
C	ARG242
C	GLN244
C	LEU288
C	HOH541
C	HOH558

site_id	AC6
Number of Residues	5
Details	binding site for residue GOL C 402

Chain	Residue
C	SER9
C	GLN20
C	PHE21
C	ASP25
C	HOH540

site_id	AC7
Number of Residues	14
Details	binding site for residue PAL D 401

Chain	Residue
D	SER62
D	SER63
D	ARG64
D	THR65
D	ARG113
D	HIS141
D	ARG174
D	ARG242
D	GLN244
D	LEU288
D	HOH505
D	HOH520
E	SER89
E	LYS92

site_id	AC8
Number of Residues	4
Details	binding site for residue GOL D 402

Chain	Residue
D	SER9
D	GLN20
D	ASP25
D	HOH535

site_id	AC9
Number of Residues	13
Details	binding site for residue PAL E 401

Chain	Residue
E	SER62
E	SER63
E	ARG64
E	THR65
E	ARG113
E	HIS141
E	ARG174
E	THR175
E	ARG242
E	GLN244
E	LEU288
E	HOH505
E	HOH538

site_id	AD1
Number of Residues	4
Details	binding site for residue GOL E 402

Chain	Residue
E	SER9
E	GLN20
E	ASP25
E	HOH547

site_id	AD2
Number of Residues	14
Details	binding site for residue PAL F 401

Chain	Residue
F	SER63
F	ARG64
F	THR65
F	ARG113
F	HIS141
F	ARG174
F	ARG242
F	GLN244
F	LEU288
F	HOH545
F	HOH547
D	SER89
D	LYS92
F	SER62

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL F 402

Chain	Residue
F	SER9
F	LEU10
F	LYS13
F	GLN20
F	ASP25
F	HOH527

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