Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8T1H

Cryo-EM structure of a full-length, native Drp1 dimer

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000266	biological_process	mitochondrial fission
A	0003924	molecular_function	GTPase activity
A	0005096	molecular_function	GTPase activator activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005741	cellular_component	mitochondrial outer membrane
A	0005777	cellular_component	peroxisome
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005794	cellular_component	Golgi apparatus
A	0005829	cellular_component	cytosol
A	0005874	cellular_component	microtubule
A	0005903	cellular_component	brush border
A	0005905	cellular_component	clathrin-coated pit
A	0006897	biological_process	endocytosis
A	0007005	biological_process	mitochondrion organization
A	0007029	biological_process	endoplasmic reticulum organization
A	0008017	molecular_function	microtubule binding
A	0008289	molecular_function	lipid binding
A	0010821	biological_process	regulation of mitochondrion organization
A	0012501	biological_process	programmed cell death
A	0012505	cellular_component	endomembrane system
A	0016020	cellular_component	membrane
A	0016559	biological_process	peroxisome fission
A	0016787	molecular_function	hydrolase activity
A	0030672	cellular_component	synaptic vesicle membrane
A	0030742	molecular_function	GTP-dependent protein binding
A	0031267	molecular_function	small GTPase binding
A	0031410	cellular_component	cytoplasmic vesicle
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043653	biological_process	mitochondrial fragmentation involved in apoptotic process
A	0048312	biological_process	intracellular distribution of mitochondria
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0048511	biological_process	rhythmic process
A	0050714	biological_process	positive regulation of protein secretion
A	0051259	biological_process	protein complex oligomerization
A	0060047	biological_process	heart contraction
A	0090023	biological_process	positive regulation of neutrophil chemotaxis
A	0090141	biological_process	positive regulation of mitochondrial fission
A	0090149	biological_process	mitochondrial membrane fission
A	0099073	cellular_component	mitochondrion-derived vesicle
A	1900063	biological_process	regulation of peroxisome organization
A	1901524	biological_process	regulation of mitophagy
A	1903532	biological_process	positive regulation of secretion by cell
A	1903578	biological_process	regulation of ATP metabolic process
B	0000166	molecular_function	nucleotide binding
B	0000266	biological_process	mitochondrial fission
B	0003924	molecular_function	GTPase activity
B	0005096	molecular_function	GTPase activator activity
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005741	cellular_component	mitochondrial outer membrane
B	0005777	cellular_component	peroxisome
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005794	cellular_component	Golgi apparatus
B	0005829	cellular_component	cytosol
B	0005874	cellular_component	microtubule
B	0005903	cellular_component	brush border
B	0005905	cellular_component	clathrin-coated pit
B	0006897	biological_process	endocytosis
B	0007005	biological_process	mitochondrion organization
B	0007029	biological_process	endoplasmic reticulum organization
B	0008017	molecular_function	microtubule binding
B	0008289	molecular_function	lipid binding
B	0010821	biological_process	regulation of mitochondrion organization
B	0012501	biological_process	programmed cell death
B	0012505	cellular_component	endomembrane system
B	0016020	cellular_component	membrane
B	0016559	biological_process	peroxisome fission
B	0016787	molecular_function	hydrolase activity
B	0030672	cellular_component	synaptic vesicle membrane
B	0030742	molecular_function	GTP-dependent protein binding
B	0031267	molecular_function	small GTPase binding
B	0031410	cellular_component	cytoplasmic vesicle
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0043653	biological_process	mitochondrial fragmentation involved in apoptotic process
B	0048312	biological_process	intracellular distribution of mitochondria
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0048511	biological_process	rhythmic process
B	0050714	biological_process	positive regulation of protein secretion
B	0051259	biological_process	protein complex oligomerization
B	0060047	biological_process	heart contraction
B	0090023	biological_process	positive regulation of neutrophil chemotaxis
B	0090141	biological_process	positive regulation of mitochondrial fission
B	0090149	biological_process	mitochondrial membrane fission
B	0099073	cellular_component	mitochondrion-derived vesicle
B	1900063	biological_process	regulation of peroxisome organization
B	1901524	biological_process	regulation of mitophagy
B	1903532	biological_process	positive regulation of secretion by cell
B	1903578	biological_process	regulation of ATP metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00410
Number of Residues	10
Details	G_DYNAMIN_1 Dynamin-type guanine nucleotide-binding (G) domain signature. LPRGTGIVTR

Chain	Residue	Details
A	LEU51-ARG60

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	560
Details	Domain: {"description":"Dynamin-type G","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	182
Details	Domain: {"description":"GED","evidences":[{"source":"PROSITE-ProRule","id":"PRU00720","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	14
Details	Region: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Region: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Region: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Region: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Region: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	290
Details	Region: {"description":"Middle domain","evidences":[{"source":"PubMed","id":"15208300","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	28
Details	Region: {"description":"Important for homodimerization","evidences":[{"source":"PubMed","id":"23584531","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	34
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23977156","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"19342591","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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