3TUT

Crystal structure of RtcA.ATP binary complex

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ATP A 401

Chain	Residue
A	GLY16
A	ALA130
A	PRO131
A	PHE251
A	TYR284
A	ASP287
A	GLN288
A	ASN309
A	HOH384
A	HOH423
A	HOH424
A	GLY17
A	HOH461
A	HOH473
A	HOH523
A	HOH555
A	HOH629
A	GLN18
A	ARG21
A	ARG40
A	ARG43
A	GLN51
A	HIS52
A	SER129

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site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 340

Chain	Residue
A	LYS45
A	LEU49
A	ARG50
A	SER95
A	HOH387
A	HOH525
A	HOH571
A	HOH633

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 341

Chain	Residue
A	ARG137
A	ARG137
A	ARG138
A	HOH524
A	HOH622

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 501

Chain	Residue
A	ARG43
A	ALA44
A	LYS45

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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	1
Details	ACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:20399182, ECO:0007744|PDB:1QMH

Chain	Residue	Details
A	ASN309

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:20399182, ECO:0007744|PDB:3KGD

Chain	Residue	Details
A	GLN104
A	PRO131
A	TYR284
A	ASP287
A	GLN288
A	ASN309

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 882

Chain	Residue	Details
A	GLU14	modifies pKa
A	ASN309	covalent catalysis

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