+Open data
-Basic information
Entry | Database: PDB / ID: 5g1a | ||||||
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Title | Bordetella Alcaligenes HDAH bound to PFSAHA | ||||||
Components | HISTONE DEACETYLASE-LIKE AMIDOHYDROLASE | ||||||
Keywords | HYDROLASE / HDAH / HDAC / HDLP | ||||||
Function / homology | Function and homology information Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / histone deacetylase activity / negative regulation of transcription by RNA polymerase II / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ALCALIGENES (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.42 Å | ||||||
Authors | Kraemer, A. / Meyer-Almes, F.J. / Yildiz, O. | ||||||
Citation | Journal: Biochim. Biophys. Acta / Year: 2017 Title: The thermodynamic signature of ligand binding to histone deacetylase-like amidohydrolases is most sensitive to the flexibility in the L2-loop lining the active site pocket. Authors: Meyners, C. / Kramer, A. / Yildiz, O. / Meyer-Almes, F.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5g1a.cif.gz | 334.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5g1a.ent.gz | 274.3 KB | Display | PDB format |
PDBx/mmJSON format | 5g1a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5g1a_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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Full document | 5g1a_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | 5g1a_validation.xml.gz | 39.4 KB | Display | |
Data in CIF | 5g1a_validation.cif.gz | 60.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g1/5g1a ftp://data.pdbj.org/pub/pdb/validation_reports/g1/5g1a | HTTPS FTP |
-Related structure data
Related structure data | 5g17C 5g1bC 5g0xS S: Starting model for refinement C: citing same article (ref.) |
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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 on special symmetry positions |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 39707.844 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ALCALIGENES (bacteria) / Strain: FB188 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): XL1 BLUE / References: UniProt: Q70I53, amidase |
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-Non-polymers , 6 types, 951 molecules
#2: Chemical | #3: Chemical | ChemComp-K / #4: Chemical | #5: Chemical | #6: Chemical | ChemComp-PEG / #7: Water | ChemComp-HOH / | |
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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: 2.9 Å3/Da / Density % sol: 57.7 % / Description: NONE |
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Crystal grow | pH: 5.25 / Details: pH 5.25 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1.00002 |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 3, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.00002 Å / Relative weight: 1 |
Reflection | Resolution: 1.42→22.7 Å / Num. obs: 168945 / % possible obs: 97.4 % / Observed criterion σ(I): 2.3 / Redundancy: 6.7 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 11.8 |
Reflection shell | Resolution: 1.42→1.44 Å / Redundancy: 7.1 % / Rmerge(I) obs: 0.87 / Mean I/σ(I) obs: 2.3 / % possible all: 95.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 5G0X Resolution: 1.42→87.96 Å / Cor.coef. Fo:Fc: 0.976 / Cor.coef. Fo:Fc free: 0.968 / SU B: 1.918 / SU ML: 0.033 / Cross valid method: THROUGHOUT / ESU R: 0.054 / ESU R Free: 0.051 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.039 Å2
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Refinement step | Cycle: LAST / Resolution: 1.42→87.96 Å
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Refine LS restraints |
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