+Open data
-Basic information
Entry | Database: PDB / ID: 1lbe | ||||||
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Title | APLYSIA ADP RIBOSYL CYCLASE | ||||||
Components | ADP RIBOSYL CYCLASE | ||||||
Keywords | HYDROLASE / NAD(+) NUCLEOSIDASE / NADASE | ||||||
Function / homology | Function and homology information 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase / phosphorus-oxygen lyase activity / NAD+ nucleosidase activity / NAD+ nucleotidase, cyclic ADP-ribose generating / Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds / single fertilization / positive regulation of B cell proliferation / transferase activity / cytoplasmic vesicle / plasma membrane Similarity search - Function | ||||||
Biological species | Aplysia californica (California sea hare) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | ||||||
Authors | Prasad, G.S. / Mcree, D.E. / Stura, E.A. / Levitt, D.G. / Lee, H.C. / Stout, C.D. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1996 Title: Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38. Authors: Prasad, G.S. / McRee, D.E. / Stura, E.A. / Levitt, D.G. / Lee, H.C. / Stout, C.D. #1: Journal: Proteins / Year: 1996 Title: Crystallization of Adp-Ribosyl Cyclase from Aplysia Californica Authors: Pradas, G.S. / Levitt, D.G. / Lee, H.C. / Stout, C.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lbe.cif.gz | 105.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lbe.ent.gz | 87.6 KB | Display | PDB format |
PDBx/mmJSON format | 1lbe.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lbe_validation.pdf.gz | 375 KB | Display | wwPDB validaton report |
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Full document | 1lbe_full_validation.pdf.gz | 395.6 KB | Display | |
Data in XML | 1lbe_validation.xml.gz | 13.2 KB | Display | |
Data in CIF | 1lbe_validation.cif.gz | 19.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lb/1lbe ftp://data.pdbj.org/pub/pdb/validation_reports/lb/1lbe | HTTPS FTP |
-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: 29579.945 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Aplysia californica (California sea hare) / Organ: OVOTESTIS / References: UniProt: P29241, NAD+ glycohydrolase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 55 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7 / Method: vapor diffusionDetails: drop solution was mixed with an equal volume of reservoir solution | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 84127 / % possible obs: 98.3 % / Observed criterion σ(I): 0 / Redundancy: 3.36 % / Rmerge(I) obs: 0.103 |
Reflection | *PLUS Highest resolution: 2.4 Å / Num. obs: 25029 / Num. measured all: 84127 |
-Processing
Software |
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Refinement | Resolution: 2.4→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 32 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |