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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8T0K

Cryo-EM of the GDP-bound human dynamin (full-length) polymer assembled on the membrane in the super constricted state

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
b0000166molecular_functionnucleotide binding
b0003723molecular_functionRNA binding
b0003924molecular_functionGTPase activity
b0005515molecular_functionprotein binding
b0005525molecular_functionGTP binding
b0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
b0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
b0005737cellular_componentcytoplasm
b0005874cellular_componentmicrotubule
b0005886cellular_componentplasma membrane
b0005905cellular_componentclathrin-coated pit
b0006897biological_processendocytosis
b0006898biological_processreceptor-mediated endocytosis
b0007032biological_processendosome organization
b0008017molecular_functionmicrotubule binding
b0016020cellular_componentmembrane
b0016185biological_processsynaptic vesicle budding from presynaptic endocytic zone membrane
b0016787molecular_functionhydrolase activity
b0019003molecular_functionGDP binding
b0019901molecular_functionprotein kinase binding
b0030139cellular_componentendocytic vesicle
b0031410cellular_componentcytoplasmic vesicle
b0042583cellular_componentchromaffin granule
b0042802molecular_functionidentical protein binding
b0042803molecular_functionprotein homodimerization activity
b0045202cellular_componentsynapse
b0051260biological_processprotein homooligomerization
b0051289biological_processprotein homotetramerization
b0070062cellular_componentextracellular exosome
b0097494biological_processregulation of vesicle size
b0098793cellular_componentpresynapse
b0099049biological_processclathrin coat assembly involved in endocytosis
b0099050biological_processvesicle scission
c0000166molecular_functionnucleotide binding
c0003723molecular_functionRNA binding
c0003924molecular_functionGTPase activity
c0005515molecular_functionprotein binding
c0005525molecular_functionGTP binding
c0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
c0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
c0005737cellular_componentcytoplasm
c0005874cellular_componentmicrotubule
c0005886cellular_componentplasma membrane
c0005905cellular_componentclathrin-coated pit
c0006897biological_processendocytosis
c0006898biological_processreceptor-mediated endocytosis
c0007032biological_processendosome organization
c0008017molecular_functionmicrotubule binding
c0016020cellular_componentmembrane
c0016185biological_processsynaptic vesicle budding from presynaptic endocytic zone membrane
c0016787molecular_functionhydrolase activity
c0019003molecular_functionGDP binding
c0019901molecular_functionprotein kinase binding
c0030139cellular_componentendocytic vesicle
c0031410cellular_componentcytoplasmic vesicle
c0042583cellular_componentchromaffin granule
c0042802molecular_functionidentical protein binding
c0042803molecular_functionprotein homodimerization activity
c0045202cellular_componentsynapse
c0051260biological_processprotein homooligomerization
c0051289biological_processprotein homotetramerization
c0070062cellular_componentextracellular exosome
c0097494biological_processregulation of vesicle size
c0098793cellular_componentpresynapse
c0099049biological_processclathrin coat assembly involved in endocytosis
c0099050biological_processvesicle scission
f0000166molecular_functionnucleotide binding
f0003723molecular_functionRNA binding
f0003924molecular_functionGTPase activity
f0005515molecular_functionprotein binding
f0005525molecular_functionGTP binding
f0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
f0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
f0005737cellular_componentcytoplasm
f0005874cellular_componentmicrotubule
f0005886cellular_componentplasma membrane
f0005905cellular_componentclathrin-coated pit
f0006897biological_processendocytosis
f0006898biological_processreceptor-mediated endocytosis
f0007032biological_processendosome organization
f0008017molecular_functionmicrotubule binding
f0016020cellular_componentmembrane
f0016185biological_processsynaptic vesicle budding from presynaptic endocytic zone membrane
f0016787molecular_functionhydrolase activity
f0019003molecular_functionGDP binding
f0019901molecular_functionprotein kinase binding
f0030139cellular_componentendocytic vesicle
f0031410cellular_componentcytoplasmic vesicle
f0042583cellular_componentchromaffin granule
f0042802molecular_functionidentical protein binding
f0042803molecular_functionprotein homodimerization activity
f0045202cellular_componentsynapse
f0051260biological_processprotein homooligomerization
f0051289biological_processprotein homotetramerization
f0070062cellular_componentextracellular exosome
f0097494biological_processregulation of vesicle size
f0098793cellular_componentpresynapse
f0099049biological_processclathrin coat assembly involved in endocytosis
f0099050biological_processvesicle scission
g0000166molecular_functionnucleotide binding
g0003723molecular_functionRNA binding
g0003924molecular_functionGTPase activity
g0005515molecular_functionprotein binding
g0005525molecular_functionGTP binding
g0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
g0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
g0005737cellular_componentcytoplasm
g0005874cellular_componentmicrotubule
g0005886cellular_componentplasma membrane
g0005905cellular_componentclathrin-coated pit
g0006897biological_processendocytosis
g0006898biological_processreceptor-mediated endocytosis
g0007032biological_processendosome organization
g0008017molecular_functionmicrotubule binding
g0016020cellular_componentmembrane
g0016185biological_processsynaptic vesicle budding from presynaptic endocytic zone membrane
g0016787molecular_functionhydrolase activity
g0019003molecular_functionGDP binding
g0019901molecular_functionprotein kinase binding
g0030139cellular_componentendocytic vesicle
g0031410cellular_componentcytoplasmic vesicle
g0042583cellular_componentchromaffin granule
g0042802molecular_functionidentical protein binding
g0042803molecular_functionprotein homodimerization activity
g0045202cellular_componentsynapse
g0051260biological_processprotein homooligomerization
g0051289biological_processprotein homotetramerization
g0070062cellular_componentextracellular exosome
g0097494biological_processregulation of vesicle size
g0098793cellular_componentpresynapse
g0099049biological_processclathrin coat assembly involved in endocytosis
g0099050biological_processvesicle scission
Functional Information from PROSITE/UniProt
site_idPS00410
Number of Residues10
DetailsG_DYNAMIN_1 Dynamin-type guanine nucleotide-binding (G) domain signature. LPRGSGIVTR
ChainResidueDetails
bLEU57-ARG66
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1064
DetailsDomain: {"description":"Dynamin-type G","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues28
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues8
DetailsRegion: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues12
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues12
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20428113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26612256","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5D3Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20428113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26612256","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X2E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X2F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D3Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20428113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26612256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30069048","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X2E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X2F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D3Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6DLU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26612256","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5D3Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20428113","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X2E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X2F","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20428113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26612256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30069048","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X2E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D3Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6DLU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues8
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P39053","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; alternate","evidences":[{"source":"UniProtKB","id":"P39053","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P39053","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P21575","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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