+Open data
-Basic information
Entry | Database: PDB / ID: 1uz3 | ||||||
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Title | Crystal structure of novel protein EMSY | ||||||
Components | EMSY PROTEIN | ||||||
Keywords | CHROMATIN REGULATOR / CHROMATIN REGULATORS / ROYAL FAMILY DOMAIN | ||||||
Function / homology | Function and homology information chromatin organization / DNA repair / regulation of DNA-templated transcription / nucleoplasm / identical protein binding Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / DIRECT METHODS / Resolution: 1.1 Å | ||||||
Authors | Chavali, G.B. / Basu, B.P. / Doherty, A.J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2005 Title: Crystal Structure of the Ent Domain of Human Emsy. Authors: Chavali, G.B. / Ekblad, C.M. / Basu, B.P. / Brissett, N.C. / Veprintsev, D. / Hughes-Davies, L. / Kouzarides, T. / Itzhaki, L.S. / Doherty, A.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uz3.cif.gz | 104.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uz3.ent.gz | 81.5 KB | Display | PDB format |
PDBx/mmJSON format | 1uz3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uz/1uz3 ftp://data.pdbj.org/pub/pdb/validation_reports/uz/1uz3 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 11475.146 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-100 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q8TE50, UniProt: Q7Z589*PLUS #2: Water | ChemComp-HOH / | Compound details | EMSY PROTEIN IS AMPLIFIED IN BREAST CANCER AND INTERACTS WITH BRCA2. THE EMSY N TERMINAL (ENT) ...EMSY PROTEIN IS AMPLIFIED IN BREAST CANCER AND INTERACTS WITH BRCA2. THE EMSY N TERMINAL (ENT) DOMAIN IS FOUND IN OTHER VERTEBRATE | Sequence details | FIRST TWO RESIDUES IN THE GIVEN IN THE SEQUENCE GLY-SER ARE FROM THE CLEAVED HIS-TAG. | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 29.3 % |
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Crystal grow | pH: 6.5 / Details: 0.1 M HEPES PH 6.5, 18% PEG 8000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX14.2 / Wavelength: 0.979 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Dec 9, 2002 / Details: MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 1.1→19.49 Å / Num. obs: 71522 / % possible obs: 99.5 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 4.3 |
Reflection shell | Resolution: 1.1→1.16 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 2.9 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: DIRECT METHODS / Resolution: 1.1→10 Å / Num. parameters: 17472 / Num. restraintsaints: 20167 / Cross valid method: FREE R-VALUE / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER / Details: RESIDUES 1, 99 AND 100 ARE DISORDERED IN CHAIN B
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Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 1941 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.1→10 Å
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Refine LS restraints |
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