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8T1H

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000266biological_processmitochondrial fission
A0003924molecular_functionGTPase activity
A0005096molecular_functionGTPase activator activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005777cellular_componentperoxisome
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005874cellular_componentmicrotubule
A0005903cellular_componentbrush border
A0005905cellular_componentclathrin-coated pit
A0006816biological_processcalcium ion transport
A0006897biological_processendocytosis
A0007005biological_processmitochondrion organization
A0007029biological_processendoplasmic reticulum organization
A0008017molecular_functionmicrotubule binding
A0008289molecular_functionlipid binding
A0010468biological_processregulation of gene expression
A0010821biological_processregulation of mitochondrion organization
A0012501biological_processprogrammed cell death
A0012505cellular_componentendomembrane system
A0016020cellular_componentmembrane
A0016559biological_processperoxisome fission
A0016787molecular_functionhydrolase activity
A0030672cellular_componentsynaptic vesicle membrane
A0030742molecular_functionGTP-dependent protein binding
A0031267molecular_functionsmall GTPase binding
A0031410cellular_componentcytoplasmic vesicle
A0031625molecular_functionubiquitin protein ligase binding
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043653biological_processmitochondrial fragmentation involved in apoptotic process
A0045202cellular_componentsynapse
A0048312biological_processintracellular distribution of mitochondria
A0048471cellular_componentperinuclear region of cytoplasm
A0048511biological_processrhythmic process
A0050714biological_processpositive regulation of protein secretion
A0051259biological_processprotein complex oligomerization
A0060047biological_processheart contraction
A0070585biological_processprotein localization to mitochondrion
A0090023biological_processpositive regulation of neutrophil chemotaxis
A0090141biological_processpositive regulation of mitochondrial fission
A0090149biological_processmitochondrial membrane fission
A0099073cellular_componentmitochondrion-derived vesicle
A0160040biological_processmitocytosis
A1900063biological_processregulation of peroxisome organization
A1901524biological_processregulation of mitophagy
A1903532biological_processpositive regulation of secretion by cell
A1903578biological_processregulation of ATP metabolic process
B0000166molecular_functionnucleotide binding
B0000266biological_processmitochondrial fission
B0003924molecular_functionGTPase activity
B0005096molecular_functionGTPase activator activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005777cellular_componentperoxisome
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0005874cellular_componentmicrotubule
B0005903cellular_componentbrush border
B0005905cellular_componentclathrin-coated pit
B0006816biological_processcalcium ion transport
B0006897biological_processendocytosis
B0007005biological_processmitochondrion organization
B0007029biological_processendoplasmic reticulum organization
B0008017molecular_functionmicrotubule binding
B0008289molecular_functionlipid binding
B0010468biological_processregulation of gene expression
B0010821biological_processregulation of mitochondrion organization
B0012501biological_processprogrammed cell death
B0012505cellular_componentendomembrane system
B0016020cellular_componentmembrane
B0016559biological_processperoxisome fission
B0016787molecular_functionhydrolase activity
B0030672cellular_componentsynaptic vesicle membrane
B0030742molecular_functionGTP-dependent protein binding
B0031267molecular_functionsmall GTPase binding
B0031410cellular_componentcytoplasmic vesicle
B0031625molecular_functionubiquitin protein ligase binding
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043653biological_processmitochondrial fragmentation involved in apoptotic process
B0045202cellular_componentsynapse
B0048312biological_processintracellular distribution of mitochondria
B0048471cellular_componentperinuclear region of cytoplasm
B0048511biological_processrhythmic process
B0050714biological_processpositive regulation of protein secretion
B0051259biological_processprotein complex oligomerization
B0060047biological_processheart contraction
B0070585biological_processprotein localization to mitochondrion
B0090023biological_processpositive regulation of neutrophil chemotaxis
B0090141biological_processpositive regulation of mitochondrial fission
B0090149biological_processmitochondrial membrane fission
B0099073cellular_componentmitochondrion-derived vesicle
B0160040biological_processmitocytosis
B1900063biological_processregulation of peroxisome organization
B1901524biological_processregulation of mitophagy
B1903532biological_processpositive regulation of secretion by cell
B1903578biological_processregulation of ATP metabolic process
Functional Information from PROSITE/UniProt
site_idPS00410
Number of Residues10
DetailsG_DYNAMIN_1 Dynamin-type guanine nucleotide-binding (G) domain signature. LPRGTGIVTR
ChainResidueDetails
ALEU51-ARG60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:23977156
ChainResidueDetails
AGLY32
ATHR215
AASN246
BGLY32
BTHR215
BASN246

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER529
BSER529

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER548
ASER607
BSER548
BSER607

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q8K1M6
ChainResidueDetails
ALYS597
BLYS597

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 and PINK1 => ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:26122121, ECO:0000269|PubMed:32484300, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER616
BSER616

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CAMK1 and PKA => ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:26122121, ECO:0000269|PubMed:32439975
ChainResidueDetails
ASER637
BSER637

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:19342591
ChainResidueDetails
ACYS644
BCYS644

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000250
ChainResidueDetails
ATHR585
ATHR586
BTHR585
BTHR586

site_idSWS_FT_FI10
Number of Residues16
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:19638400
ChainResidueDetails
ALYS532
BLYS535
BLYS558
BLYS568
BLYS594
BLYS606
BLYS608
ALYS535
ALYS558
ALYS568
ALYS594
ALYS606
ALYS608
BLYS532

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
ChainResidueDetails
ALYS597
BLYS597

238268

PDB entries from 2025-07-02

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