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- PDB-1jwg: VHS Domain of human GGA1 complexed with cation-independent M6PR C... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1jwg | ||||||
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Title | VHS Domain of human GGA1 complexed with cation-independent M6PR C-terminal Peptide | ||||||
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![]() | PROTEIN TRANSPORT/PROTEIN BINDING / SUPER HELIX / PROTEIN-PEPTIDE COMPLEX / PROTEIN TRANSPORT-PROTEIN BINDING COMPLEX | ||||||
Function / homology | ![]() protein localization to ciliary membrane / Retrograde transport at the Trans-Golgi-Network / clathrin coat / retromer complex binding / response to tetrachloromethane / insulin-like growth factor receptor activity / insulin-like growth factor binding / Golgi to plasma membrane transport / insulin-like growth factor II binding / Golgi to plasma membrane protein transport ...protein localization to ciliary membrane / Retrograde transport at the Trans-Golgi-Network / clathrin coat / retromer complex binding / response to tetrachloromethane / insulin-like growth factor receptor activity / insulin-like growth factor binding / Golgi to plasma membrane transport / insulin-like growth factor II binding / Golgi to plasma membrane protein transport / trans-Golgi network transport vesicle / positive regulation by host of viral process / retinoic acid binding / retrograde transport, endosome to Golgi / protein localization to cell surface / TBC/RABGAPs / lysosomal transport / Golgi Associated Vesicle Biogenesis / nuclear envelope lumen / D-mannose binding / endocytic vesicle / G-protein alpha-subunit binding / animal organ regeneration / response to retinoic acid / transport vesicle / phosphatidylinositol binding / receptor-mediated endocytosis / post-embryonic development / secretory granule membrane / trans-Golgi network membrane / liver development / ubiquitin binding / phosphoprotein binding / intracellular protein transport / clathrin-coated endocytic vesicle membrane / protein catabolic process / trans-Golgi network / protein localization / small GTPase binding / positive regulation of protein catabolic process / late endosome / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / signaling receptor activity / early endosome membrane / spermatogenesis / early endosome / endosome membrane / endosome / positive regulation of apoptotic process / G protein-coupled receptor signaling pathway / Amyloid fiber formation / Golgi membrane / intracellular membrane-bounded organelle / focal adhesion / Neutrophil degranulation / perinuclear region of cytoplasm / Golgi apparatus / enzyme binding / cell surface / signal transduction / protein-containing complex / extracellular exosome / nucleoplasm / identical protein binding / membrane / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Shiba, T. / Takatsu, H. / Nogi, T. / Matsugaki, N. / Kawasaki, M. / Igarashi, N. / Suzuki, M. / Kato, R. / Earnest, T. / Nakayama, K. / Wakatsuki, S. | ||||||
![]() | ![]() Title: Structural basis for recognition of acidic-cluster dileucine sequence by GGA1. Authors: Shiba, T. / Takatsu, H. / Nogi, T. / Matsugaki, N. / Kawasaki, M. / Igarashi, N. / Suzuki, M. / Kato, R. / Earnest, T. / Nakayama, K. / Wakatsuki, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75.6 KB | Display | ![]() |
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PDB format | ![]() | 56.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 387.2 KB | Display | ![]() |
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Full document | ![]() | 392.8 KB | Display | |
Data in XML | ![]() | 7.5 KB | Display | |
Data in CIF | ![]() | 12.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1jwfSC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 16814.436 Da / Num. of mol.: 2 / Fragment: VHS DOMAIN(N-terminal domain) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 1544.577 Da / Num. of mol.: 2 / Fragment: C-terminal fragment / Source method: obtained synthetically / Details: This sequence occurs naturally in humans. / References: UniProt: P11717 #3: Chemical | ChemComp-IOD / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 51.74 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 3350, ammonium iodide, Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Aug 16, 2001 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. all: 24632 / Num. obs: 24632 / % possible obs: 99.6 % |
Reflection shell | Resolution: 2→2.11 Å / % possible all: 99.3 |
Reflection | *PLUS Num. obs: 25975 / Num. measured all: 167862 / Rmerge(I) obs: 0.067 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1JWF Resolution: 2→30 Å / Cor.coef. Fo:Fc: 0.933 / SU B: 4.254 / SU ML: 0.121 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.194 / ESU R Free: 0.171 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 39.099 Å2
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.052 Å / Total num. of bins used: 20
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Refinement | *PLUS Highest resolution: 2 Å / σ(F): 0 / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.05 Å / Rfactor Rfree: 0.272 / Rfactor Rwork: 0.234 |