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- PDB-5m5v: Clathrin heavy chain N-terminal domain bound to a clathrin-box mo... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5m5v | ||||||||||||
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Title | Clathrin heavy chain N-terminal domain bound to a clathrin-box motif from hepatitis D virus large antigen (clade 2) | ||||||||||||
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![]() | ENDOCYTOSIS / hepatitis delta virus / HDAg-L | ||||||||||||
Function / homology | ![]() Retrograde neurotrophin signalling / Recycling pathway of L1 / WNT5A-dependent internalization of FZD4 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / LDL clearance / Gap junction degradation / Formation of annular gap junctions / Golgi Associated Vesicle Biogenesis / RHOU GTPase cycle / RHOV GTPase cycle ...Retrograde neurotrophin signalling / Recycling pathway of L1 / WNT5A-dependent internalization of FZD4 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / LDL clearance / Gap junction degradation / Formation of annular gap junctions / Golgi Associated Vesicle Biogenesis / RHOU GTPase cycle / RHOV GTPase cycle / clathrin coat of trans-Golgi network vesicle / Lysosome Vesicle Biogenesis / clathrin light chain binding / negative regulation of hyaluronan biosynthetic process / clathrin complex / MHC class II antigen presentation / VLDLR internalisation and degradation / clathrin coat of coated pit / Cargo recognition for clathrin-mediated endocytosis / clathrin coat disassembly / clathrin coat assembly / clathrin-coated endocytic vesicle / membrane coat / Clathrin-mediated endocytosis / arrestin family protein binding / receptor-mediated endocytosis / intracellular protein transport / autophagy / spindle / viral penetration into host nucleus / host cell / disordered domain specific binding / melanosome / mitotic cell cycle / symbiont entry into host cell / protein domain specific binding / cell division / structural molecule activity / mitochondrion / RNA binding / extracellular exosome / identical protein binding Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Muenzner, J. / Graham, S.C. | ||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Cellular and viral peptides bind multiple sites on the N-terminal domain of clathrin. Authors: Muenzner, J. / Traub, L.M. / Kelly, B.T. / Graham, S.C. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 309.4 KB | Display | ![]() |
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PDB format | ![]() | 251.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 489 KB | Display | ![]() |
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Full document | ![]() | 493.2 KB | Display | |
Data in XML | ![]() | 33.6 KB | Display | |
Data in CIF | ![]() | 50.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5m5rC ![]() 5m5sC ![]() 5m5tC ![]() 5m5uC ![]() 5m61C ![]() 1c9iS 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 on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Ens-ID: 1 / Beg auth comp-ID: ILE / Beg label comp-ID: ILE / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: _ / Auth seq-ID: 4 - 363 / Label seq-ID: 6 - 365
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Components
#1: Antibody | Mass: 40540.473 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: N-terminal residues 'GS' are residual following cleavage of the purification tag Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 1012.181 Da / Num. of mol.: 6 / Fragment: Clathrin-box like motif, UNP Residues 203-209 / Source method: obtained synthetically Details: N- and C-terminal serine residues are non-natural and were added to enhance solubility Source: (synth.) ![]() #3: Chemical | ChemComp-GOL / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.64 Å3/Da / Density % sol: 66.19 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 200 nL protein:peptide (20 mg/mL NTD and 3.6 mM peptide) plus 400 nL reservoir equilibrated against a 80 uL reservoir of 1.75 M sodium malonate pH 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Oct 7, 2013 / Details: KB mirrors |
Radiation | Monochromator: Si(111) crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97949 Å / Relative weight: 1 |
Reflection | Resolution: 1.96→39.2 Å / Num. obs: 79976 / % possible obs: 94.6 % / Redundancy: 2.5 % / CC1/2: 0.996 / Rmerge(I) obs: 0.081 / Net I/σ(I): 7.2 |
Reflection shell | Resolution: 1.96→2 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.581 / Mean I/σ(I) obs: 1.5 / CC1/2: 0.563 / % possible all: 95.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1C9I Resolution: 1.96→39.2 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.958 / SU B: 5.697 / SU ML: 0.082 / Cross valid method: THROUGHOUT / ESU R: 0.119 / ESU R Free: 0.112 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.338 Å2
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Refinement step | Cycle: 1 / Resolution: 1.96→39.2 Å
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Refine LS restraints |
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