Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8EFV

Structure of single homo-hexameric Holliday junction ATP-dependent DNA helicase RuvB motor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000400	molecular_function	four-way junction DNA binding
A	0003677	molecular_function	DNA binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006281	biological_process	DNA repair
A	0006310	biological_process	DNA recombination
A	0006974	biological_process	DNA damage response
A	0009378	molecular_function	four-way junction helicase activity
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0048476	cellular_component	Holliday junction resolvase complex
B	0000166	molecular_function	nucleotide binding
B	0000400	molecular_function	four-way junction DNA binding
B	0003677	molecular_function	DNA binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006281	biological_process	DNA repair
B	0006310	biological_process	DNA recombination
B	0006974	biological_process	DNA damage response
B	0009378	molecular_function	four-way junction helicase activity
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0048476	cellular_component	Holliday junction resolvase complex
C	0000166	molecular_function	nucleotide binding
C	0000400	molecular_function	four-way junction DNA binding
C	0003677	molecular_function	DNA binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006281	biological_process	DNA repair
C	0006310	biological_process	DNA recombination
C	0006974	biological_process	DNA damage response
C	0009378	molecular_function	four-way junction helicase activity
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0048476	cellular_component	Holliday junction resolvase complex
D	0000166	molecular_function	nucleotide binding
D	0000400	molecular_function	four-way junction DNA binding
D	0003677	molecular_function	DNA binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006281	biological_process	DNA repair
D	0006310	biological_process	DNA recombination
D	0006974	biological_process	DNA damage response
D	0009378	molecular_function	four-way junction helicase activity
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0048476	cellular_component	Holliday junction resolvase complex
E	0000166	molecular_function	nucleotide binding
E	0000400	molecular_function	four-way junction DNA binding
E	0003677	molecular_function	DNA binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006281	biological_process	DNA repair
E	0006310	biological_process	DNA recombination
E	0006974	biological_process	DNA damage response
E	0009378	molecular_function	four-way junction helicase activity
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0048476	cellular_component	Holliday junction resolvase complex
F	0000166	molecular_function	nucleotide binding
F	0000400	molecular_function	four-way junction DNA binding
F	0003677	molecular_function	DNA binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006281	biological_process	DNA repair
F	0006310	biological_process	DNA recombination
F	0006974	biological_process	DNA damage response
F	0009378	molecular_function	four-way junction helicase activity
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0048476	cellular_component	Holliday junction resolvase complex

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	420
Details	Region: {"description":"Small ATPAse domain (RuvB-S)","evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11171970","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11171970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HQC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1IXS","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11171970","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HQC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1IXS","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IXR","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IXR","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1IXS","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11171970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HQC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1IXS","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 780

Chain	Residue	Details
A	LYS51
A	THR52
A	ASP97
A	THR146	electrostatic stabiliser
A	ARG205	electrostatic stabiliser

site_id	MCSA2
Number of Residues	5
Details	M-CSA 780

Chain	Residue	Details
B	LYS51
B	THR52
B	ASP97
B	THR146	electrostatic stabiliser
B	ARG205	electrostatic stabiliser

site_id	MCSA3
Number of Residues	5
Details	M-CSA 780

Chain	Residue	Details
C	LYS51
C	THR52
C	ASP97
C	THR146	electrostatic stabiliser
C	ARG205	electrostatic stabiliser

site_id	MCSA4
Number of Residues	5
Details	M-CSA 780

Chain	Residue	Details
D	LYS51
D	THR52
D	ASP97
D	THR146	electrostatic stabiliser
D	ARG205	electrostatic stabiliser

site_id	MCSA5
Number of Residues	5
Details	M-CSA 780

Chain	Residue	Details
E	LYS51
E	THR52
E	ASP97
E	THR146	electrostatic stabiliser
E	ARG205	electrostatic stabiliser

site_id	MCSA6
Number of Residues	5
Details	M-CSA 780

Chain	Residue	Details
F	LYS51
F	THR52
F	ASP97
F	THR146	electrostatic stabiliser
F	ARG205	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)