6LT7

Crystal structure of human RPP20-RPP25 proteins in complex with the P3 domain of lncRNA RMRP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000172	cellular_component	ribonuclease MRP complex
A	0001682	biological_process	tRNA 5'-leader removal
A	0003676	molecular_function	nucleic acid binding
A	0003723	molecular_function	RNA binding
A	0004526	molecular_function	ribonuclease P activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005655	cellular_component	nucleolar ribonuclease P complex
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0006364	biological_process	rRNA processing
A	0006396	biological_process	RNA processing
A	0008033	biological_process	tRNA processing
A	0030681	cellular_component	multimeric ribonuclease P complex
A	0033204	molecular_function	ribonuclease P RNA binding
A	0043231	cellular_component	intracellular membrane-bounded organelle
B	0000172	cellular_component	ribonuclease MRP complex
B	0001682	biological_process	tRNA 5'-leader removal
B	0003676	molecular_function	nucleic acid binding
B	0003723	molecular_function	RNA binding
B	0004526	molecular_function	ribonuclease P activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005730	cellular_component	nucleolus
B	0006364	biological_process	rRNA processing
B	0008033	biological_process	tRNA processing
B	0030681	cellular_component	multimeric ribonuclease P complex
B	0033204	molecular_function	ribonuclease P RNA binding
B	0034451	cellular_component	centriolar satellite
D	0000172	cellular_component	ribonuclease MRP complex
D	0001682	biological_process	tRNA 5'-leader removal
D	0003676	molecular_function	nucleic acid binding
D	0003723	molecular_function	RNA binding
D	0004526	molecular_function	ribonuclease P activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005655	cellular_component	nucleolar ribonuclease P complex
D	0005730	cellular_component	nucleolus
D	0005737	cellular_component	cytoplasm
D	0006364	biological_process	rRNA processing
D	0006396	biological_process	RNA processing
D	0008033	biological_process	tRNA processing
D	0030681	cellular_component	multimeric ribonuclease P complex
D	0033204	molecular_function	ribonuclease P RNA binding
D	0043231	cellular_component	intracellular membrane-bounded organelle
E	0000172	cellular_component	ribonuclease MRP complex
E	0001682	biological_process	tRNA 5'-leader removal
E	0003676	molecular_function	nucleic acid binding
E	0003723	molecular_function	RNA binding
E	0004526	molecular_function	ribonuclease P activity
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005730	cellular_component	nucleolus
E	0006364	biological_process	rRNA processing
E	0008033	biological_process	tRNA processing
E	0030681	cellular_component	multimeric ribonuclease P complex
E	0033204	molecular_function	ribonuclease P RNA binding
E	0034451	cellular_component	centriolar satellite

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue EDO A 201

Chain	Residue
A	ASN126
A	EDO202
A	HOH332
A	HOH344

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site_id	AC2
Number of Residues	5
Details	binding site for residue EDO A 202

Chain	Residue
A	ASN126
A	EDO201
A	HOH333
E	ARG87
F	U36

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site_id	AC3
Number of Residues	2
Details	binding site for residue EDO B 201

Chain	Residue
B	ARG87
D	ASN126

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site_id	AC4
Number of Residues	5
Details	binding site for residue EDO C 201

Chain	Residue
A	HIS72
A	HIS131
C	A30
C	HOH303
C	HOH327

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site_id	AC5
Number of Residues	3
Details	binding site for residue EDO C 202

Chain	Residue
C	U51
C	C52
C	G68

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site_id	AC6
Number of Residues	1
Details	binding site for residue EDO E 201

Chain	Residue
E	HOH320

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231

Chain	Residue	Details
B	SER172
E	SER172

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
B	SER182
E	SER182

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