+Open data
-Basic information
Entry | Database: PDB / ID: 2igp | ||||||
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Title | Crystal Structure of Hec1 CH domain | ||||||
Components | Retinoblastoma-associated protein HEC | ||||||
Keywords | CELL CYCLE / calponin homology (CH) domain / alpha helices | ||||||
Function / homology | Function and homology information G2/MI transition of meiotic cell cycle / kinetochore adaptor activity / skeletal muscle satellite cell proliferation / Ndc80 complex / kinetochore organization / metaphase chromosome alignment / positive regulation of mitotic cell cycle spindle assembly checkpoint / attachment of spindle microtubules to kinetochore / outer kinetochore / attachment of mitotic spindle microtubules to kinetochore ...G2/MI transition of meiotic cell cycle / kinetochore adaptor activity / skeletal muscle satellite cell proliferation / Ndc80 complex / kinetochore organization / metaphase chromosome alignment / positive regulation of mitotic cell cycle spindle assembly checkpoint / attachment of spindle microtubules to kinetochore / outer kinetochore / attachment of mitotic spindle microtubules to kinetochore / spindle assembly involved in female meiosis I / mitotic spindle assembly checkpoint signaling / mitotic sister chromatid segregation / establishment of mitotic spindle orientation / centrosome duplication / chromosome, centromeric region / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / cyclin binding / mitotic spindle organization / chromosome segregation / RHO GTPases Activate Formins / regulation of protein stability / kinetochore / Separation of Sister Chromatids / mitotic cell cycle / microtubule binding / cell division / centrosome / nucleoplasm / membrane / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.8 Å | ||||||
Authors | Wei, R.R. / Harrison, S.C. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2007 Title: The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment. Authors: Wei, R.R. / Al-Bassam, J. / Harrison, S.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2igp.cif.gz | 37.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2igp.ent.gz | 25.7 KB | Display | PDB format |
PDBx/mmJSON format | 2igp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ig/2igp ftp://data.pdbj.org/pub/pdb/validation_reports/ig/2igp | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 13800.016 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HEC1 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta pLyS / References: UniProt: O14777 | ||
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#2: Chemical | #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: 2.25 Å3/Da / Density % sol: 45.42 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.1 M cacodylate, pH 6.5, 22-30% PEG 8K, 0.2 M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 1.8→50 Å / Num. obs: 12129 / % possible obs: 100 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 7 % / Biso Wilson estimate: 18.1 Å2 / Rmerge(I) obs: 0.075 / Rsym value: 0.075 / Net I/σ(I): 26.7 | ||||||||||||||||||
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 4.25 / Num. unique all: 1208 / Rsym value: 0.33 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.8→37.37 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.926 / SU B: 2.536 / SU ML: 0.081 / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / ESU R: 0.135 / ESU R Free: 0.126 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.801 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→37.37 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.847 Å / Total num. of bins used: 20
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