Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2FZC

The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.10 Resolution

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	0009347	cellular_component	aspartate carbamoyltransferase complex
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	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
B	0006221	biological_process	pyrimidine nucleotide biosynthetic process
B	0008270	molecular_function	zinc ion binding
B	0009347	cellular_component	aspartate carbamoyltransferase complex
B	0046872	molecular_function	metal ion binding
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	0009347	cellular_component	aspartate carbamoyltransferase complex
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	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
D	0006221	biological_process	pyrimidine nucleotide biosynthetic process
D	0008270	molecular_function	zinc ion binding
D	0009347	cellular_component	aspartate carbamoyltransferase complex
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 154

Chain	Residue
B	CYS109
B	CYS114
B	CYS138
B	CYS141

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 154

Chain	Residue
D	CYS109
D	CYS114
D	CYS138
D	CYS141

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE EOP A 811

Chain	Residue
A	ARG54
A	THR55
A	ARG105
A	HIS134
A	GLN137
A	ARG167
A	THR168
A	PRO266
A	LEU267
A	HOH873
A	HOH902
A	SER52

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EOP C 812

Chain	Residue
C	SER52
C	ARG54
C	THR55
C	ARG105
C	HIS134
C	GLN137
C	ARG167
C	THR168
C	ARG229
C	HOH927
C	HOH1069

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CTP B 901

Chain	Residue
B	THR2
B	ALA11
B	ILE12
B	VAL17
B	ASP19
B	HIS20
B	LYS60
B	ASN84
B	ILE86
B	TYR89
B	VAL91
B	LYS94
B	ALA131
B	HOH912
B	HOH924
B	HOH933
B	HOH957
B	HOH964

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CTP D 902

Chain	Residue
D	ALA11
D	VAL17
D	ASP19
D	HIS20
D	LEU58
D	LYS60
D	ASN84
D	TYR89
D	VAL91
D	HOH903
D	HOH913
D	HOH929
D	HOH931
D	HOH963
D	HOH988
D	HOH989
D	HOH1025

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	8
Details	BINDING:

Chain	Residue	Details
B	CYS109
C	HIS106
C	PRO135
C	THR138
C	PRO268
C	ARG269
B	CYS114
B	CYS138
B	CYS141
D	CYS109
D	CYS114
D	CYS138
D	CYS141
C	ARG56

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00001, ECO:0000305\|PubMed:3380787

Chain	Residue	Details
A	GLY85
A	THR168
A	VAL230
C	GLY85
C	THR168
C	VAL230

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1at1

Chain	Residue	Details
A	ARG54
A	HIS134
A	ARG105
A	THR55

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1at1

Chain	Residue	Details
C	ARG54
C	HIS134
C	ARG105
C	THR55

site_id	MCSA1
Number of Residues	5
Details	M-CSA 405

Chain	Residue	Details
A	THR55	electrostatic stabiliser
A	ARG56	electrostatic stabiliser, increase electrophilicity
A	GLY85	proton shuttle (general acid/base)
A	HIS106	electrostatic stabiliser, increase electrophilicity
A	PRO135	electrostatic stabiliser, increase electrophilicity

site_id	MCSA2
Number of Residues	5
Details	M-CSA 405

Chain	Residue	Details
C	THR55	electrostatic stabiliser
C	ARG56	electrostatic stabiliser, increase electrophilicity
C	GLY85	proton shuttle (general acid/base)
C	HIS106	electrostatic stabiliser, increase electrophilicity
C	PRO135	electrostatic stabiliser, increase electrophilicity

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