2AT1

CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH

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	PMA
Number of Residues	10
Details	BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.

Chain	Residue
A	ARG54
A	LEU267
A	THR55
A	ARG105
A	HIS134
A	GLN137
A	ARG167
A	ARG229
A	GLN231
A	PRO266

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site_id	PMC
Number of Residues	10
Details	BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.

Chain	Residue
C	ARG54
C	THR55
C	ARG105
C	HIS134
C	GLN137
C	ARG167
C	ARG229
C	GLN231
C	PRO266
C	LEU267

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site_id	ZNB
Number of Residues	4
Details	zn binding site

Chain	Residue
B	CYS109
B	CYS114
B	CYS138
B	CYS141

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site_id	ZND
Number of Residues	4
Details	zn binding site

Chain	Residue
D	CYS109
D	CYS114
D	CYS138
D	CYS141

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
B	PRO110
B	ILE115
B	LYS139
B	GLU142
D	PRO110
D	ILE115
D	LYS139
D	GLU142
C	HIS106
C	PRO135
C	THR138
C	PRO268
C	ARG269
C	ARG56

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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

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Catalytic Information from CSA

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

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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

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