1NBE

ASPARTATE TRANSCARBAMOYLASE REGULATORY CHAIN MUTANT (T82A)

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	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	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

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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

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MLT A 311

Chain	Residue
A	THR55
A	ARG105
A	HIS134
A	ARG167
A	PRO266
A	LEU267
A	HOH385
A	ARG54

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MLT A 312

Chain	Residue
A	GLN231
A	ARG234
A	HOH452
A	HOH457

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site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MLT C 311

Chain	Residue
C	SER52
C	THR55
C	ARG105
C	HIS134
C	GLN137
C	ARG167
C	HOH321
C	HOH434
C	HOH504

---

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MLT C 312

Chain	Residue
C	ASP162
C	TYR165
C	GLN231
C	ARG234
C	HOH341
C	HOH343
C	HOH435
C	HOH476
C	HOH485
C	HOH516
C	HOH523

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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	14
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3380787","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3380787","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

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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	ARG54	electrostatic stabiliser
A	THR55	electrostatic stabiliser, increase electrophilicity
A	LYS84	proton shuttle (general acid/base)
A	ARG105	electrostatic stabiliser, increase electrophilicity
A	HIS134	electrostatic stabiliser, increase electrophilicity

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 405

Chain	Residue	Details
C	ARG54	electrostatic stabiliser
C	THR55	electrostatic stabiliser, increase electrophilicity
C	LYS84	proton shuttle (general acid/base)
C	ARG105	electrostatic stabiliser, increase electrophilicity
C	HIS134	electrostatic stabiliser, increase electrophilicity

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