+Open data
-Basic information
Entry | Database: PDB / ID: 1h7c | |||||||||
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Title | human tubulin chaperone cofactor a | |||||||||
Components | TUBULIN-SPECIFIC CHAPERONE A | |||||||||
Keywords | CHAPERONE / TUBULIN / PROTEIN FOLDING / COFACTOR A / P14 | |||||||||
Function / homology | Function and homology information post-chaperonin tubulin folding pathway / Post-chaperonin tubulin folding pathway / tubulin complex assembly / beta-tubulin binding / tubulin binding / microtubule cytoskeleton / protein folding / protein-folding chaperone binding / microtubule / nucleolus ...post-chaperonin tubulin folding pathway / Post-chaperonin tubulin folding pathway / tubulin complex assembly / beta-tubulin binding / tubulin binding / microtubule cytoskeleton / protein folding / protein-folding chaperone binding / microtubule / nucleolus / RNA binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | HOMO SAPIENS (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.8 Å | |||||||||
Authors | Guasch, A. / Aloria, K. / Perez, R. / Campo, R. / Avila, J. / Zabala, J.C. / Coll, M. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 2002 Title: Three-Dimensional Structure of Human Tubulin Chaperone Cofactor A Authors: Guasch, A. / Aloria, K. / Perez, R. / Avila, J. / Zabala, J.C. / Coll, M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1h7c.cif.gz | 33.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1h7c.ent.gz | 25.9 KB | Display | PDB format |
PDBx/mmJSON format | 1h7c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h7/1h7c ftp://data.pdbj.org/pub/pdb/validation_reports/h7/1h7c | 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: 13168.367 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Organ: BRAIN / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: O75347 |
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#2: Chemical | ChemComp-ACY / |
#3: Chemical | ChemComp-SO4 / |
#4: 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: 1.99 Å3/Da / Density % sol: 38.09 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.00 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6.6 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.978808 |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 15, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.978808 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→20 Å / Num. obs: 34789 / % possible obs: 99.6 % / Observed criterion σ(I): 1 / Redundancy: 2.5 % / Rsym value: 0.046 |
Reflection shell | Resolution: 1.8→2 Å / Rsym value: 0.046 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 37.3 Å / Num. obs: 7295 / % possible obs: 99.9 % / Redundancy: 3.4 % / Num. measured all: 25086 / Rmerge(I) obs: 0.04 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.06 Å / % possible obs: 99.9 % / Redundancy: 2.7 % / Rmerge(I) obs: 0.081 / Mean I/σ(I) obs: 8.1 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.8→100 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.8→100 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 37.3 Å / % reflection Rfree: 10 % / Rfactor obs: 0.21 / Rfactor Rfree: 0.262 / Rfactor Rwork: 0.21 / Highest resolution: 2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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