Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6JKS

Crystal structure of aspartate transcarbamoylase from Trypanosoma cruzi in complex with carbamoyl phosphate (CP) and aspartate (Asp)

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	12
Details	binding site for residue CP A 401

Chain	Residue
A	SER62
A	ASP402
B	SER89
B	LYS92
A	SER63
A	ARG64
A	THR65
A	ARG113
A	HIS141
A	GLN144
A	PRO287
A	LEU288

site_id	AC2
Number of Residues	10
Details	binding site for residue ASP A 402

Chain	Residue
A	ARG113
A	ARG174
A	ARG242
A	GLN244
A	LEU288
A	PRO289
A	CP401
A	HOH543
A	HOH549
B	LYS92

site_id	AC3
Number of Residues	12
Details	binding site for residue CP B 401

Chain	Residue
B	SER62
B	SER63
B	ARG64
B	THR65
B	ARG113
B	HIS141
B	GLN144
B	PRO287
B	LEU288
B	ASP402
C	SER89
C	LYS92

site_id	AC4
Number of Residues	9
Details	binding site for residue ASP B 402

Chain	Residue
B	ARG113
B	ARG174
B	THR175
B	ARG242
B	LEU288
B	PRO289
B	CP401
B	HOH569
C	LYS92

site_id	AC5
Number of Residues	11
Details	binding site for residue CP C 401

Chain	Residue
A	SER89
C	SER62
C	SER63
C	ARG64
C	THR65
C	ARG113
C	HIS141
C	GLN144
C	PRO287
C	LEU288
C	ASP402

site_id	AC6
Number of Residues	9
Details	binding site for residue ASP C 402

Chain	Residue
A	LYS92
C	ARG113
C	HIS141
C	ARG174
C	ARG242
C	GLN244
C	LEU288
C	PRO289
C	CP401

site_id	AC7
Number of Residues	12
Details	binding site for residue CP D 401

Chain	Residue
D	SER62
D	SER63
D	ARG64
D	THR65
D	ARG113
D	HIS141
D	GLN144
D	PRO287
D	LEU288
D	ASP402
E	SER89
E	HOH502

site_id	AC8
Number of Residues	11
Details	binding site for residue ASP D 402

Chain	Residue
D	ARG113
D	ARG174
D	THR175
D	ARG242
D	GLN244
D	LEU288
D	PRO289
D	CP401
D	HOH502
D	HOH538
E	LYS92

site_id	AC9
Number of Residues	12
Details	binding site for residue CP E 401

Chain	Residue
E	SER62
E	SER63
E	ARG64
E	THR65
E	ARG113
E	HIS141
E	GLN144
E	PRO287
E	LEU288
E	ASP402
F	SER89
F	LYS92

site_id	AD1
Number of Residues	10
Details	binding site for residue ASP E 402

Chain	Residue
E	HIS141
E	ARG174
E	THR175
E	ARG242
E	GLN244
E	LEU288
E	PRO289
E	CP401
E	HOH567
E	ARG113

site_id	AD2
Number of Residues	12
Details	binding site for residue CP F 401

Chain	Residue
D	SER89
D	LYS92
F	SER62
F	SER63
F	ARG64
F	THR65
F	ARG113
F	HIS141
F	GLN144
F	PRO287
F	LEU288
F	ASP402

site_id	AD3
Number of Residues	9
Details	binding site for residue ASP F 402

Chain	Residue
F	ARG113
F	HIS141
F	ARG174
F	THR175
F	ARG242
F	GLN244
F	LEU288
F	PRO289
F	CP401

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