Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6STY

Human REXO2 exonuclease in complex with RNA.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000175	molecular_function	3'-5'-RNA exonuclease activity
A	0000287	molecular_function	magnesium ion binding
A	0003676	molecular_function	nucleic acid binding
A	0004527	molecular_function	exonuclease activity
A	0005634	cellular_component	nucleus
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005758	cellular_component	mitochondrial intermembrane space
A	0005759	cellular_component	mitochondrial matrix
A	0005925	cellular_component	focal adhesion
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006259	biological_process	DNA metabolic process
A	0008296	molecular_function	3'-5'-DNA exonuclease activity
A	0008408	molecular_function	3'-5' exonuclease activity
A	0009117	biological_process	nucleotide metabolic process
A	0046872	molecular_function	metal ion binding
B	0000175	molecular_function	3'-5'-RNA exonuclease activity
B	0000287	molecular_function	magnesium ion binding
B	0003676	molecular_function	nucleic acid binding
B	0004527	molecular_function	exonuclease activity
B	0005634	cellular_component	nucleus
B	0005730	cellular_component	nucleolus
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005758	cellular_component	mitochondrial intermembrane space
B	0005759	cellular_component	mitochondrial matrix
B	0005925	cellular_component	focal adhesion
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006259	biological_process	DNA metabolic process
B	0008296	molecular_function	3'-5'-DNA exonuclease activity
B	0008408	molecular_function	3'-5' exonuclease activity
B	0009117	biological_process	nucleotide metabolic process
B	0046872	molecular_function	metal ion binding
D	0000175	molecular_function	3'-5'-RNA exonuclease activity
D	0000287	molecular_function	magnesium ion binding
D	0003676	molecular_function	nucleic acid binding
D	0004527	molecular_function	exonuclease activity
D	0005634	cellular_component	nucleus
D	0005730	cellular_component	nucleolus
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005758	cellular_component	mitochondrial intermembrane space
D	0005759	cellular_component	mitochondrial matrix
D	0005925	cellular_component	focal adhesion
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006259	biological_process	DNA metabolic process
D	0008296	molecular_function	3'-5'-DNA exonuclease activity
D	0008408	molecular_function	3'-5' exonuclease activity
D	0009117	biological_process	nucleotide metabolic process
D	0046872	molecular_function	metal ion binding
E	0000175	molecular_function	3'-5'-RNA exonuclease activity
E	0000287	molecular_function	magnesium ion binding
E	0003676	molecular_function	nucleic acid binding
E	0004527	molecular_function	exonuclease activity
E	0005634	cellular_component	nucleus
E	0005730	cellular_component	nucleolus
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005758	cellular_component	mitochondrial intermembrane space
E	0005759	cellular_component	mitochondrial matrix
E	0005925	cellular_component	focal adhesion
E	0006139	biological_process	nucleobase-containing compound metabolic process
E	0006259	biological_process	DNA metabolic process
E	0008296	molecular_function	3'-5'-DNA exonuclease activity
E	0008408	molecular_function	3'-5' exonuclease activity
E	0009117	biological_process	nucleotide metabolic process
E	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue CA B 301

Chain	Residue
B	ASP47
C	U1
C	C2

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:30926754, ECO:0000269\|PubMed:31588022

Chain	Residue	Details
A	HIS194
B	HIS194
D	HIS194
E	HIS194

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:30926754, ECO:0000269\|PubMed:31588022, ECO:0007744\|PDB:6J7Y, ECO:0007744\|PDB:6RCN

Chain	Residue	Details
A	ASP47
A	GLU49
B	ASP47
B	GLU49
D	ASP47
D	GLU49
E	ASP47
E	GLU49

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:30926754, ECO:0000269\|PubMed:31588022, ECO:0007744\|PDB:6RCN

Chain	Residue	Details
A	ASP147
B	ASP147
D	ASP147
E	ASP147

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:30926754, ECO:0007744\|PDB:6J7Y

Chain	Residue	Details
A	ASP199
B	ASP199
D	ASP199
E	ASP199

site_id	SWS_FT_FI5
Number of Residues	12
Details	SITE: Important for dinucleotide binding => ECO:0000269\|PubMed:30926754, ECO:0000269\|PubMed:32365187

Chain	Residue	Details
A	LEU53
E	LEU53
E	TRP96
E	TYR164
A	TRP96
A	TYR164
B	LEU53
B	TRP96
B	TYR164
D	LEU53
D	TRP96
D	TYR164

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER92
B	SER92
D	SER92
E	SER92

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455

Chain	Residue	Details
A	TYR122
B	TYR122
D	TYR122
E	TYR122

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q9D8S4

Chain	Residue	Details
A	LYS173
B	LYS173
D	LYS173
E	LYS173

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