+Open data
-Basic information
Entry | Database: PDB / ID: 1cf4 | ||||||
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Title | CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX | ||||||
Components |
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Keywords | TRANSFERASE / CDC42-ACK GTPASE COMPLEX / G PROTEIN | ||||||
Function / homology | Function and homology information regulation of clathrin-dependent endocytosis / GBD domain binding / submandibular salivary gland formation / actin filament branching / Golgi transport complex / positive regulation of pinocytosis / modification of synaptic structure / endothelin receptor signaling pathway involved in heart process / Cdc42 protein signal transduction / cytoophidium ...regulation of clathrin-dependent endocytosis / GBD domain binding / submandibular salivary gland formation / actin filament branching / Golgi transport complex / positive regulation of pinocytosis / modification of synaptic structure / endothelin receptor signaling pathway involved in heart process / Cdc42 protein signal transduction / cytoophidium / cardiac neural crest cell migration involved in outflow tract morphogenesis / positive regulation of synapse structural plasticity / Grb2-EGFR complex / dendritic cell migration / storage vacuole / GTPase inhibitor activity / apolipoprotein A-I receptor binding / positive regulation of epithelial cell proliferation involved in lung morphogenesis / neuron fate determination / modulation by host of viral process / organelle transport along microtubule / regulation of attachment of spindle microtubules to kinetochore / positive regulation of pseudopodium assembly / WW domain binding / Inactivation of CDC42 and RAC1 / cardiac conduction system development / GTP-dependent protein binding / regulation of filopodium assembly / establishment of Golgi localization / leading edge membrane / neuropilin signaling pathway / positive regulation of intracellular protein transport / cell junction assembly / filopodium assembly / establishment of epithelial cell apical/basal polarity / regulation of modification of postsynaptic structure / dendritic spine morphogenesis / mitogen-activated protein kinase kinase kinase binding / embryonic heart tube development / thioesterase binding / regulation of stress fiber assembly / RHO GTPases activate KTN1 / regulation of lamellipodium assembly / nuclear migration / DCC mediated attractive signaling / adherens junction organization / sprouting angiogenesis / Wnt signaling pathway, planar cell polarity pathway / CD28 dependent Vav1 pathway / regulation of postsynapse organization / positive regulation of filopodium assembly / clathrin-coated vesicle / regulation of mitotic nuclear division / establishment or maintenance of cell polarity / phagocytosis, engulfment / RHOV GTPase cycle / small GTPase-mediated signal transduction / epidermal growth factor receptor binding / heart contraction / Myogenesis / RHOJ GTPase cycle / Golgi organization / RHOQ GTPase cycle / positive regulation of cytokinesis / RHO GTPases activate PAKs / CDC42 GTPase cycle / RHOU GTPase cycle / macrophage differentiation / RHOG GTPase cycle / RHO GTPases Activate WASPs and WAVEs / RAC3 GTPase cycle / RAC2 GTPase cycle / RHO GTPases activate IQGAPs / spindle midzone / negative regulation of protein-containing complex assembly / phagocytic vesicle / positive regulation of lamellipodium assembly / positive regulation of substrate adhesion-dependent cell spreading / clathrin-coated pit / positive regulation of stress fiber assembly / GPVI-mediated activation cascade / RAC1 GTPase cycle / EPHB-mediated forward signaling / substantia nigra development / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / protein serine/threonine/tyrosine kinase activity / small monomeric GTPase / G protein activity / filopodium / positive regulation of DNA replication / secretory granule / actin filament organization / integrin-mediated signaling pathway / RHO GTPases Activate Formins / regulation of actin cytoskeleton organization / FCGR3A-mediated phagocytosis / adherens junction / EGFR downregulation / positive regulation of JNK cascade / non-specific protein-tyrosine kinase Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING | ||||||
Authors | Mott, H.R. / Owen, D. / Nietlispach, D. / Lowe, P.N. / Lim, L. / Laue, E.D. | ||||||
Citation | Journal: Nature / Year: 1999 Title: Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK. Authors: Mott, H.R. / Owen, D. / Nietlispach, D. / Lowe, P.N. / Manser, E. / Lim, L. / Laue, E.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cf4.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1cf4.ent.gz | 1.1 MB | Display | PDB format |
PDBx/mmJSON format | 1cf4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cf/1cf4 ftp://data.pdbj.org/pub/pdb/validation_reports/cf/1cf4 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 20438.555 Da / Num. of mol.: 1 / Mutation: Q61L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P60953 |
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#2: Protein/peptide | Mass: 4844.192 Da / Num. of mol.: 1 / Fragment: GTPASE-BINDING DOMAIN / Source method: isolated from a natural source / Details: COMPLEXED WITH 5'-GUANOSYL-IMIDO-TRIPHOSPHATE / Source: (natural) Homo sapiens (human) / References: UniProt: Q07912 |
#3: Chemical | ChemComp-MG / |
#4: Chemical | ChemComp-GNP / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | pH: 5.5 / Temperature: 298.0 K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: medoid | ||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 20 |