1ACM

ARGININE 54 IN THE ACTIVE SITE OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE IS CRITICAL FOR CATALYSIS: A SITE-SPECIFIC MUTAGENESIS, NMR AND X-RAY CRYSTALLOGRAPHY STUDY

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	15
Details	BINDING SITE FOR RESIDUE PAL A 311

Chain	Residue
A	SER52
A	THR53
A	ALA54
A	THR55
A	SER80
A	LYS84
A	ARG105
A	HIS134
A	GLN137
A	ARG167
A	ARG229
A	GLN231
A	LEU267
A	PRO268
A	HOH315

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PAL C 311

Chain	Residue
C	SER52
C	THR53
C	ALA54
C	THR55
C	SER80
C	LYS84
C	ARG105
C	HIS134
C	ARG167
C	ARG229
C	GLN231
C	LEU267
C	PRO268
C	HOH316

---

site_id	PAA
Number of Residues	9
Details	PAL BINDING SITES OF CHAINS A

Chain	Residue
A	SER52
A	ALA54
A	THR55
A	SER80
A	LYS84
A	HIS134
A	ARG167
A	ARG229
A	GLN231

---

site_id	PAC
Number of Residues	9
Details	PAL BINDING SITES OF CHAINS C

Chain	Residue
C	SER52
C	ALA54
C	THR55
C	SER80
C	LYS84
C	HIS134
C	ARG167
C	ARG229
C	GLN231

---

site_id	ZNB
Number of Residues	4
Details	ZN BINDING SITES OF CHAINS B

Chain	Residue
B	CYS109
B	CYS114
B	CYS138
B	CYS141

---

site_id	ZND
Number of Residues	4
Details	ZN BINDING SITES OF CHAINS D

Chain	Residue
D	CYS109
D	CYS114
D	CYS138
D	CYS141

---

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

---

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	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

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