Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8JHK

Cryo-EM structure of the DOCK5/ELMO1 complex, focused on one protomer

Functional Information from GO Data
ChainGOidnamespacecontents
A0005085molecular_functionguanyl-nucleotide exchange factor activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006909biological_processphagocytosis
A0006911biological_processphagocytosis, engulfment
A0006915biological_processapoptotic process
A0007015biological_processactin filament organization
A0016020cellular_componentmembrane
A0016601biological_processRac protein signal transduction
A0017124molecular_functionSH3 domain binding
A0030036biological_processactin cytoskeleton organization
A0032045cellular_componentguanyl-nucleotide exchange factor complex
A0048870biological_processcell motility
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0150052biological_processregulation of postsynapse assembly
A0160124molecular_functionguanyl nucleotide exchange factor activator activity
A2001212biological_processregulation of vasculogenesis
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005096molecular_functionGTPase activator activity
B0007264biological_processsmall GTPase-mediated signal transduction
B0016477biological_processcell migration
E0005085molecular_functionguanyl-nucleotide exchange factor activity
E0005096molecular_functionGTPase activator activity
E0007264biological_processsmall GTPase-mediated signal transduction
E0016477biological_processcell migration
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues173
DetailsDomain: {"description":"ELMO","evidences":[{"source":"PROSITE-ProRule","id":"PRU00664","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues121
DetailsDomain: {"description":"PH"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsMotif: {"description":"SH3-binding"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsModified residue: {"description":"Phosphotyrosine; by HCK","evidences":[{"source":"PubMed","id":"15952790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BPU7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues61
DetailsDomain: {"description":"SH3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00192","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues184
DetailsDomain: {"description":"C2 DOCK-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00983","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues411
DetailsDomain: {"description":"DOCKER","evidences":[{"source":"PROSITE-ProRule","id":"PRU00984","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon