+Open data
-Basic information
Entry | Database: PDB / ID: 1w1w | ||||||
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Title | Sc Smc1hd:Scc1-C complex, ATPgS | ||||||
Components |
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Keywords | CELL ADHESION / COHESIN / CHROMOSOME SEGREGATION / KLEISIN / MITOSIS / CELL CYCLE | ||||||
Function / homology | Function and homology information Establishment of Sister Chromatid Cohesion / Resolution of Sister Chromatid Cohesion / meiotic cohesin complex / establishment of meiotic sister chromatid cohesion / mitotic cohesin complex / DNA secondary structure binding / cohesin complex / SUMOylation of DNA damage response and repair proteins / replication-born double-strand break repair via sister chromatid exchange / establishment of mitotic sister chromatid cohesion ...Establishment of Sister Chromatid Cohesion / Resolution of Sister Chromatid Cohesion / meiotic cohesin complex / establishment of meiotic sister chromatid cohesion / mitotic cohesin complex / DNA secondary structure binding / cohesin complex / SUMOylation of DNA damage response and repair proteins / replication-born double-strand break repair via sister chromatid exchange / establishment of mitotic sister chromatid cohesion / mitotic chromosome condensation / sister chromatid cohesion / mitotic sister chromatid cohesion / protein acetylation / minor groove of adenine-thymine-rich DNA binding / mitotic sister chromatid segregation / chromosome, centromeric region / condensed nuclear chromosome / double-strand break repair / double-stranded DNA binding / cell division / apoptotic process / DNA damage response / chromatin binding / protein kinase binding / ATP hydrolysis activity / mitochondrion / DNA binding / ATP binding / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2.9 Å | ||||||
Authors | Haering, C. / Nasmyth, K. / Lowe, J. | ||||||
Citation | Journal: Mol. Cell / Year: 2004 Title: Structure and stability of cohesin's Smc1-kleisin interaction. Authors: Haering, C.H. / Schoffnegger, D. / Nishino, T. / Helmhart, W. / Nasmyth, K. / Lowe, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1w1w.cif.gz | 321.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1w1w.ent.gz | 257.5 KB | Display | PDB format |
PDBx/mmJSON format | 1w1w.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1w1w_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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Full document | 1w1w_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 1w1w_validation.xml.gz | 60.8 KB | Display | |
Data in CIF | 1w1w_validation.cif.gz | 81.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w1/1w1w ftp://data.pdbj.org/pub/pdb/validation_reports/w1/1w1w | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 48855.023 Da / Num. of mol.: 4 / Fragment: HEAD DOMAIN RESIDUES 1-214,1024-1225 Source method: isolated from a genetically manipulated source Details: RESIDUES 1-214, ESSKHPTSLVPRGS LINKER, 1024-1225 Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P32908 #2: Protein | Mass: 13746.589 Da / Num. of mol.: 4 / Fragment: C-TERMINAL DOMAIN RESIDUES 451-563 Source method: isolated from a genetically manipulated source Details: RESIDUES 451-566 Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q12158 #3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-AGS / |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.93 Å3/Da / Density % sol: 64 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.9762 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9762 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→57 Å / Num. obs: 59522 / % possible obs: 99 % / Observed criterion σ(I): 0 / Redundancy: 6 % / Biso Wilson estimate: 86 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 15.1 |
Reflection shell | Resolution: 2.9→3.06 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 4.2 / % possible all: 97 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.9→50 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Bsol: 29.9012 Å2 / ksol: 0.314107 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 66.24 Å2
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Refinement step | Cycle: LAST / Resolution: 2.9→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.9→2.92 Å / Rfactor Rfree: 0.3937 / Rfactor Rwork: 0.3969 / Total num. of bins used: 50 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
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