+Open data
-Basic information
Entry | Database: PDB / ID: 4ne3 | ||||||
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Title | Human MHF1-MHF2 complex | ||||||
Components |
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Keywords | DNA BINDING PROTEIN / Histone fold / DNA repair / genome maintenance / Fanconi Anemia / FancM | ||||||
Function / homology | Function and homology information FANCM-MHF complex / Fanconi anaemia nuclear complex / resolution of meiotic recombination intermediates / kinetochore assembly / inner kinetochore / replication fork processing / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / interstrand cross-link repair / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation ...FANCM-MHF complex / Fanconi anaemia nuclear complex / resolution of meiotic recombination intermediates / kinetochore assembly / inner kinetochore / replication fork processing / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / interstrand cross-link repair / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Deposition of new CENPA-containing nucleosomes at the centromere / Resolution of Sister Chromatid Cohesion / positive regulation of protein ubiquitination / chromosome segregation / RHO GTPases Activate Formins / Fanconi Anemia Pathway / PKR-mediated signaling / Separation of Sister Chromatids / protein heterodimerization activity / cell division / DNA repair / DNA damage response / chromatin binding / chromatin / DNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8007 Å | ||||||
Authors | Zhao, Q. / Saro, D. / Sachpatzidis, A. / Sung, P. / Xiong, Y. | ||||||
Citation | Journal: Nat Commun / Year: 2014 Title: The MHF complex senses branched DNA by binding a pair of crossover DNA duplexes. Authors: Zhao, Q. / Saro, D. / Sachpatzidis, A. / Singh, T.R. / Schlingman, D. / Zheng, X.F. / Mack, A. / Tsai, M.S. / Mochrie, S. / Regan, L. / Meetei, A.R. / Sung, P. / Xiong, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4ne3.cif.gz | 42.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4ne3.ent.gz | 32.9 KB | Display | PDB format |
PDBx/mmJSON format | 4ne3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ne/4ne3 ftp://data.pdbj.org/pub/pdb/validation_reports/ne/4ne3 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 10739.987 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: APITD1, CENPS, FAAP16, MHF1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Rossetta / References: UniProt: Q8N2Z9 |
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#2: Protein | Mass: 8445.690 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: STRA13, CENPX, FAAP10, MHF2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Rossetta / References: UniProt: A8MT69 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.38 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.8007→28.102 Å / Num. all: 16522 / Num. obs: 16358 / % possible obs: 99.01 % / Observed criterion σ(F): 0 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.8007→28.102 Å / Occupancy max: 1 / Occupancy min: 0.47 / FOM work R set: 0.8007 / SU ML: 0.24 / σ(F): 0 / Phase error: 27.05 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Shrinkage radii: 1.06 Å / VDW probe radii: 1.3 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 61.375 Å2 / ksol: 0.409 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 92.75 Å2 / Biso mean: 39.9791 Å2 / Biso min: 18.14 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8007→28.102 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 6
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