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- PDB-1gyw: Gamma-adaptin appendage domain from clathrin adaptor AP1 A753D mutant -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gyw | ||||||
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Title | Gamma-adaptin appendage domain from clathrin adaptor AP1 A753D mutant | ||||||
![]() | ADAPTER-RELATED PROTEIN COMPLEX 1 GAMMA 1 SUBUNIT | ||||||
![]() | ENDOCYTOSIS / ADAPTOR / COATED PITS | ||||||
Function / homology | ![]() basolateral protein secretion / AP-1 adaptor complex / Lysosome Vesicle Biogenesis / platelet dense granule organization / melanosome assembly / Golgi to vacuole transport / Golgi Associated Vesicle Biogenesis / clathrin adaptor activity / MHC class II antigen presentation / clathrin-coated vesicle ...basolateral protein secretion / AP-1 adaptor complex / Lysosome Vesicle Biogenesis / platelet dense granule organization / melanosome assembly / Golgi to vacuole transport / Golgi Associated Vesicle Biogenesis / clathrin adaptor activity / MHC class II antigen presentation / clathrin-coated vesicle / clathrin-coated pit / vesicle-mediated transport / trans-Golgi network membrane / intracellular protein transport / trans-Golgi network / early endosome / lysosomal membrane / perinuclear region of cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Evans, P.R. / Miele, A.E. / Owen, D.J. / McMahon, H.M. / Kent, H.M. | ||||||
![]() | ![]() Title: Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin. Authors: Kent, H.M. / McMahon, H.T. / Evans, P.R. / Benmerah, A. / Owen, D.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.2 KB | Display | ![]() |
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PDB format | ![]() | 48 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 417.7 KB | Display | ![]() |
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Full document | ![]() | 420.2 KB | Display | |
Data in XML | ![]() | 12.9 KB | Display | |
Data in CIF | ![]() | 18.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gyuSC ![]() 1gyvC 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.134391, 0.511664, 0.84861), Vector: |
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Components
#1: Protein | Mass: 14255.128 Da / Num. of mol.: 2 / Fragment: APPENDAGE DOMAIN, RESIDUES 694-821 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-CL / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 55.9 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion / pH: 8 Details: 24% PEG4000, 100 MM TRIS PH 8.0, 200MM MGCL2, VAPOUR DIFFUSION | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 15, 2001 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54182 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→23.06 Å / Num. obs: 11979 / % possible obs: 99.3 % / Observed criterion σ(I): 6 / Redundancy: 13.62 % / Rmerge(I) obs: 0.086 / Net I/σ(I): 8.1922 |
Reflection shell | Resolution: 2.4→2.53 Å / Redundancy: 13.41 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 2.18 / % possible all: 96.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: WILD-TYPE 1GYU Resolution: 2.4→57.74 Å / SU B: 7.025 / SU ML: 0.166 / Cross valid method: THROUGHOUT / ESU R Free: 0.288 / Details: NONE
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Displacement parameters | Biso mean: 27.773 Å2
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Refinement step | Cycle: LAST / Resolution: 2.4→57.74 Å
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LS refinement shell | *PLUS Highest resolution: 2.404 Å / Lowest resolution: 2.467 Å / Rfactor Rfree: 0.266 / Rfactor Rwork: 0.235 / Total num. of bins used: 20 |