+Open data
-Basic information
Entry | Database: PDB / ID: 6j3a | ||||||
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Title | Structure of LmbA2991HD | ||||||
Components | Gamma-glutamyltranspeptidase | ||||||
Keywords | TRANSFERASE / LmbA2991 / GGT2991 / LmbA-like glutamyltranspeptidase homologues | ||||||
Function / homology | Gamma-glutamyltranspeptidase / Gamma-glutamyltranspeptidase, large subunit, C-terminal domain / Gamma-glutamyltranspeptidase, small subunit / Nucleophile aminohydrolases, N-terminal / transferase activity / Gamma-glutamyltransferase family protein Function and homology information | ||||||
Biological species | Streptomyces lincolnensis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.38 Å | ||||||
Authors | Song, Y. | ||||||
Funding support | China, 1items
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Citation | Journal: To Be Published Title: Structure of LmbA2991HD Authors: Song, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6j3a.cif.gz | 222.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6j3a.ent.gz | 178.2 KB | Display | PDB format |
PDBx/mmJSON format | 6j3a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j3/6j3a ftp://data.pdbj.org/pub/pdb/validation_reports/j3/6j3a | HTTPS FTP |
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-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: 65153.270 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces lincolnensis (bacteria) / Gene: SLCG_6815, SLINC_6827 / Production host: Escherichia coli K-12 (bacteria) / Strain (production host): K-12 / References: UniProt: A0A1B1MKD3 #2: 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: 2.44 Å3/Da / Density % sol: 49.59 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / Details: 0.1M Tris pH8.0, 28% w/v Polyethylene glycol 4000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.9785 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jan 15, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9785 Å / Relative weight: 1 |
Reflection | Resolution: 2.38→81.19 Å / Num. obs: 51650 / % possible obs: 99.4 % / Redundancy: 5.4 % / Net I/σ(I): 8.33 |
Reflection shell | Resolution: 2.38→2.42 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.38→50 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.921 / SU B: 13.125 / SU ML: 0.276 / Cross valid method: THROUGHOUT / ESU R: 0.435 / ESU R Free: 0.275 / 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: 33.72 Å2
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Refinement step | Cycle: 1 / Resolution: 2.38→50 Å
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Refine LS restraints |
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