1QMI

Crystal structure of RNA 3'-terminal phosphate cyclase, an ubiquitous enzyme with unusual topology

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003963	molecular_function	RNA-3'-phosphate cyclase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006396	biological_process	RNA processing
A	0016874	molecular_function	ligase activity
B	0003824	molecular_function	catalytic activity
B	0003963	molecular_function	RNA-3'-phosphate cyclase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006396	biological_process	RNA processing
B	0016874	molecular_function	ligase activity
C	0003824	molecular_function	catalytic activity
C	0003963	molecular_function	RNA-3'-phosphate cyclase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006396	biological_process	RNA processing
C	0016874	molecular_function	ligase activity
D	0003824	molecular_function	catalytic activity
D	0003963	molecular_function	RNA-3'-phosphate cyclase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006396	biological_process	RNA processing
D	0016874	molecular_function	ligase activity

Functional Information from PROSITE/UniProt

site_id	PS01287
Number of Residues	11
Details	RTC RNA 3'-terminal phosphate cyclase signature. HGfyPaGGGvV

Chain	Residue	Details
A	HIS158-VAL168

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:20399182, ECO:0007744|PDB:1QMH

Chain	Residue	Details
A	HIS309
B	HIS309
C	HIS309
D	HIS309

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site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:20399182, ECO:0007744|PDB:3KGD

Chain	Residue	Details
A	GLN104
B	ASP287
B	GLN288
B	HIS309
C	GLN104
C	PRO131
C	TYR284
C	ASP287
C	GLN288
C	HIS309
D	GLN104
A	PRO131
D	PRO131
D	TYR284
D	ASP287
D	GLN288
D	HIS309
A	TYR284
A	ASP287
A	GLN288
A	HIS309
B	GLN104
B	PRO131
B	TYR284

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Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS309

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

Chain	Residue	Details
B	HIS309

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site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1qmh

Chain	Residue	Details
C	HIS309

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site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1qmh

Chain	Residue	Details
D	HIS309

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 882

Chain	Residue	Details
A	GLU14	modifies pKa
A	HIS309	covalent catalysis

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site_id	MCSA2
Number of Residues	2
Details	M-CSA 882

Chain	Residue	Details
B	GLU14	modifies pKa
B	HIS309	covalent catalysis

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site_id	MCSA3
Number of Residues	2
Details	M-CSA 882

Chain	Residue	Details
C	GLU14	modifies pKa
C	HIS309	covalent catalysis

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site_id	MCSA4
Number of Residues	2
Details	M-CSA 882

Chain	Residue	Details
D	GLU14	modifies pKa
D	HIS309	covalent catalysis

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