Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5HZG

The crystal structure of the strigolactone-induced AtD14-D3-ASK1 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0010223	biological_process	secondary shoot formation
A	0016787	molecular_function	hydrolase activity
A	1901601	biological_process	strigolactone biosynthetic process
A	1902348	biological_process	cellular response to strigolactone
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0009653	biological_process	anatomical structure morphogenesis
B	0019005	cellular_component	SCF ubiquitin ligase complex
B	0031146	biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
B	0050793	biological_process	regulation of developmental process
B	0061137	biological_process	bud dilation
B	1900618	biological_process	regulation of shoot system morphogenesis
C	0000151	cellular_component	ubiquitin ligase complex
C	0000226	biological_process	microtubule cytoskeleton organization
C	0000278	biological_process	mitotic cell cycle
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005819	cellular_component	spindle
C	0005829	cellular_component	cytosol
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0007059	biological_process	chromosome segregation
C	0007140	biological_process	male meiotic nuclear division
C	0009524	cellular_component	phragmoplast
C	0009733	biological_process	response to auxin
C	0009734	biological_process	auxin-activated signaling pathway
C	0009753	biological_process	response to jasmonic acid
C	0009867	biological_process	jasmonic acid mediated signaling pathway
C	0009873	biological_process	ethylene-activated signaling pathway
C	0016567	biological_process	protein ubiquitination
C	0031146	biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
C	0045910	biological_process	negative regulation of DNA recombination
C	0097602	molecular_function	cullin family protein binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0010223	biological_process	secondary shoot formation
E	0016787	molecular_function	hydrolase activity
E	1901601	biological_process	strigolactone biosynthetic process
E	1902348	biological_process	cellular response to strigolactone
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0009653	biological_process	anatomical structure morphogenesis
F	0019005	cellular_component	SCF ubiquitin ligase complex
F	0031146	biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
F	0050793	biological_process	regulation of developmental process
F	0061137	biological_process	bud dilation
F	1900618	biological_process	regulation of shoot system morphogenesis
G	0000151	cellular_component	ubiquitin ligase complex
G	0000226	biological_process	microtubule cytoskeleton organization
G	0000278	biological_process	mitotic cell cycle
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0005739	cellular_component	mitochondrion
G	0005819	cellular_component	spindle
G	0005829	cellular_component	cytosol
G	0006511	biological_process	ubiquitin-dependent protein catabolic process
G	0007059	biological_process	chromosome segregation
G	0007140	biological_process	male meiotic nuclear division
G	0009524	cellular_component	phragmoplast
G	0009733	biological_process	response to auxin
G	0009734	biological_process	auxin-activated signaling pathway
G	0009753	biological_process	response to jasmonic acid
G	0009867	biological_process	jasmonic acid mediated signaling pathway
G	0009873	biological_process	ethylene-activated signaling pathway
G	0016567	biological_process	protein ubiquitination
G	0031146	biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
G	0045910	biological_process	negative regulation of DNA recombination
G	0097602	molecular_function	cullin family protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue 6OM A 301

Chain	Residue
A	PHE28
A	SER97
A	VAL98
A	HIS247

site_id	AC2
Number of Residues	5
Details	binding site for residue 6OM E 301

Chain	Residue
E	PHE28
E	HIS96
E	SER97
E	VAL98
E	HIS247

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"23381136","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25425668","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"23381136","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	46
Details	Repeat: {"description":"LRR 2"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	60
Details	Repeat: {"description":"LRR 3"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	56
Details	Repeat: {"description":"LRR 4"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	56
Details	Repeat: {"description":"LRR 5"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	62
Details	Repeat: {"description":"LRR 6"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	54
Details	Repeat: {"description":"LRR 8"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	27
Details	Repeat: {"description":"LRR 9"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	25
Details	Repeat: {"description":"LRR 10"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	72
Details	Repeat: {"description":"LRR 11"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	32
Details	Repeat: {"description":"LRR 12"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	66
Details	Repeat: {"description":"LRR 15"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	68
Details	Repeat: {"description":"LRR 16"}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	74
Details	Repeat: {"description":"LRR 17"}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	116
Details	Region: {"description":"Interaction with the F-box domain of F-box proteins","evidences":[{"source":"PubMed","id":"17410169","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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