+Open data
-Basic information
Entry | Database: PDB / ID: 1kao | ||||||
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Title | CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAP2A WITH GDP | ||||||
Components | RAP2A | ||||||
Keywords | GTP-BINDING PROTEIN / SMALL G PROTEIN / RAP2 / GDP / RAS | ||||||
Function / homology | Function and homology information Rap protein signal transduction / microvillus assembly / regulation of synapse assembly / regulation of dendrite morphogenesis / regulation of postsynaptic membrane neurotransmitter receptor levels / regulation of JNK cascade / positive regulation of protein autophosphorylation / small monomeric GTPase / negative regulation of cell migration / protein localization to plasma membrane ...Rap protein signal transduction / microvillus assembly / regulation of synapse assembly / regulation of dendrite morphogenesis / regulation of postsynaptic membrane neurotransmitter receptor levels / regulation of JNK cascade / positive regulation of protein autophosphorylation / small monomeric GTPase / negative regulation of cell migration / protein localization to plasma membrane / synaptic membrane / establishment of protein localization / Schaffer collateral - CA1 synapse / recycling endosome / G protein activity / recycling endosome membrane / GDP binding / protein localization / cellular response to xenobiotic stimulus / midbody / actin cytoskeleton organization / positive regulation of protein phosphorylation / GTPase activity / GTP binding / magnesium ion binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Cherfils, J. / Menetrey, J. / Le Bras, G. | ||||||
Citation | Journal: EMBO J. / Year: 1997 Title: Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPgammaS. Authors: Cherfils, J. / Menetrey, J. / Le Bras, G. / Janoueix-Lerosey, I. / de Gunzburg, J. / Garel, J.R. / Auzat, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kao.cif.gz | 48.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1kao.ent.gz | 33.6 KB | Display | PDB format |
PDBx/mmJSON format | 1kao.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1kao_validation.pdf.gz | 787.7 KB | Display | wwPDB validaton report |
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Full document | 1kao_full_validation.pdf.gz | 789.8 KB | Display | |
Data in XML | 1kao_validation.xml.gz | 9.6 KB | Display | |
Data in CIF | 1kao_validation.cif.gz | 12.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ka/1kao ftp://data.pdbj.org/pub/pdb/validation_reports/ka/1kao | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 18945.562 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P10114 | ||||
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#2: Chemical | #3: Chemical | ChemComp-GDP / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.92 Å3/Da / Density % sol: 29.6 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8 Details: PEG 6000 (25%), TRIS 100MM PH 8, MGCL2 100MM, pH 8.0 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 1.7→30 Å / Num. obs: 15836 / % possible obs: 92.8 % / Redundancy: 8 % / Biso Wilson estimate: 12.82 Å2 / Rmerge(I) obs: 0.071 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: RAS-GDP Rfactor Rwork: 0.186 / Rfactor obs: 0.186 / Highest resolution: 1.7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 14.77 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.7 Å
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Refine LS restraints |
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