Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1OYP

Crystal Structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0000175	molecular_function	3'-5'-RNA exonuclease activity
A	0003723	molecular_function	RNA binding
A	0006364	biological_process	rRNA processing
A	0008033	biological_process	tRNA processing
A	0009022	molecular_function	tRNA nucleotidyltransferase activity
A	0016075	biological_process	rRNA catabolic process
A	0016779	molecular_function	nucleotidyltransferase activity
A	0031125	biological_process	rRNA 3'-end processing
B	0000049	molecular_function	tRNA binding
B	0000175	molecular_function	3'-5'-RNA exonuclease activity
B	0003723	molecular_function	RNA binding
B	0006364	biological_process	rRNA processing
B	0008033	biological_process	tRNA processing
B	0009022	molecular_function	tRNA nucleotidyltransferase activity
B	0016075	biological_process	rRNA catabolic process
B	0016779	molecular_function	nucleotidyltransferase activity
B	0031125	biological_process	rRNA 3'-end processing
C	0000049	molecular_function	tRNA binding
C	0000175	molecular_function	3'-5'-RNA exonuclease activity
C	0003723	molecular_function	RNA binding
C	0006364	biological_process	rRNA processing
C	0008033	biological_process	tRNA processing
C	0009022	molecular_function	tRNA nucleotidyltransferase activity
C	0016075	biological_process	rRNA catabolic process
C	0016779	molecular_function	nucleotidyltransferase activity
C	0031125	biological_process	rRNA 3'-end processing
D	0000049	molecular_function	tRNA binding
D	0000175	molecular_function	3'-5'-RNA exonuclease activity
D	0003723	molecular_function	RNA binding
D	0006364	biological_process	rRNA processing
D	0008033	biological_process	tRNA processing
D	0009022	molecular_function	tRNA nucleotidyltransferase activity
D	0016075	biological_process	rRNA catabolic process
D	0016779	molecular_function	nucleotidyltransferase activity
D	0031125	biological_process	rRNA 3'-end processing
E	0000049	molecular_function	tRNA binding
E	0000175	molecular_function	3'-5'-RNA exonuclease activity
E	0003723	molecular_function	RNA binding
E	0006364	biological_process	rRNA processing
E	0008033	biological_process	tRNA processing
E	0009022	molecular_function	tRNA nucleotidyltransferase activity
E	0016075	biological_process	rRNA catabolic process
E	0016779	molecular_function	nucleotidyltransferase activity
E	0031125	biological_process	rRNA 3'-end processing
F	0000049	molecular_function	tRNA binding
F	0000175	molecular_function	3'-5'-RNA exonuclease activity
F	0003723	molecular_function	RNA binding
F	0006364	biological_process	rRNA processing
F	0008033	biological_process	tRNA processing
F	0009022	molecular_function	tRNA nucleotidyltransferase activity
F	0016075	biological_process	rRNA catabolic process
F	0016779	molecular_function	nucleotidyltransferase activity
F	0031125	biological_process	rRNA 3'-end processing

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 301

Chain	Residue
A	ARG86
A	GLY124
A	THR125
A	ARG126

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 302

Chain	Residue
A	TRP58
A	THR60
A	ARG99

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 303

Chain	Residue
B	THR125
B	ARG126
B	ARG86
B	GLY124

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 304

Chain	Residue
B	TRP58
B	THR60
B	ARG99

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 305

Chain	Residue
C	ARG86
C	GLY124
C	THR125
C	ARG126

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 306

Chain	Residue
C	TRP58
C	THR60
C	ARG99

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 307

Chain	Residue
D	ARG86
D	GLY124
D	THR125
D	ARG126

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 308

Chain	Residue
D	TRP58
D	THR60
D	ARG99

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 309

Chain	Residue
E	ARG86
E	GLY124
E	THR125
E	ARG126

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 310

Chain	Residue
E	TRP58
E	THR60
E	ARG99

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 F 311

Chain	Residue
F	ARG86
F	GLY124
F	THR125
F	ARG126

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 F 312

Chain	Residue
F	TRP58
F	THR60
F	ARG99

Functional Information from PROSITE/UniProt

site_id	PS01277
Number of Residues	13
Details	RIBONUCLEASE_PH Ribonuclease PH signature. CDVIQADGGtr.TA

Chain	Residue	Details
A	CYS116-ALA128

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00564

Chain	Residue	Details
A	ARG86
B	ARG86
C	ARG86
D	ARG86
E	ARG86
F	ARG86

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00564, ECO:0000305\|PubMed:14767080

Chain	Residue	Details
A	GLY124
B	GLY124
C	GLY124
D	GLY124
E	GLY124
F	GLY124

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)