+Open data
-Basic information
Entry | Database: PDB / ID: 1c44 | ||||||
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Title | STEROL CARRIER PROTEIN 2 (SCP2) FROM RABBIT | ||||||
Components | PROTEIN (STEROL CARRIER PROTEIN 2) | ||||||
Keywords | LIPID BINDING PROTEIN / STEROL CARRIER PROTEIN / NON SPECIFIC LIPID TRANSFER PROTEIN / FATTY ACID BINDING / FATTY ACYL COA BINDING | ||||||
Function / homology | Function and homology information propanoyl-CoA C-acyltransferase activity / propionyl-CoA C2-trimethyltridecanoyltransferase activity / acetyl-CoA C-myristoyltransferase activity / phosphatidylcholine transfer activity / propanoyl-CoA C-acyltransferase / acetyl-CoA C-acyltransferase activity / cholesterol transfer activity / bile acid metabolic process / lipid transport / fatty acid beta-oxidation ...propanoyl-CoA C-acyltransferase activity / propionyl-CoA C2-trimethyltridecanoyltransferase activity / acetyl-CoA C-myristoyltransferase activity / phosphatidylcholine transfer activity / propanoyl-CoA C-acyltransferase / acetyl-CoA C-acyltransferase activity / cholesterol transfer activity / bile acid metabolic process / lipid transport / fatty acid beta-oxidation / peroxisomal matrix / peroxisome / lipid binding / mitochondrion Similarity search - Function | ||||||
Biological species | Oryctolagus cuniculus (rabbit) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 1.8 Å | ||||||
Authors | Choinowski, T. / Hauser, H. / Piontek, K. | ||||||
Citation | Journal: Biochemistry / Year: 2000 Title: Structure of sterol carrier protein 2 at 1.8 A resolution reveals a hydrophobic tunnel suitable for lipid binding. Authors: Choinowski, T. / Hauser, H. / Piontek, K. #1: Journal: Acta Crystallogr.,Sect.D / Year: 1999 Title: Crystallization and initial X-ray analysis of rabbit mature sterol carrier protein 2 Authors: Choinowski, T. / Dyer, J.H. / Maderegger, B. / Winterhalter, K.P. / Hauser, H. / Piontek, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1c44.cif.gz | 37.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1c44.ent.gz | 27 KB | Display | PDB format |
PDBx/mmJSON format | 1c44.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c4/1c44 ftp://data.pdbj.org/pub/pdb/validation_reports/c4/1c44 | 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 13211.375 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Organ: LIVER / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: O62742 |
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#2: 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: 2.7 Å3/Da / Density % sol: 54.5 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: AMMONIUM SULFATE, LITHIUM SULFATE, CITRATE PH=6.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion | ||||||||||||||||||||||||||||||
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: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.8345 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 15, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8345 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→18 Å / Num. obs: 14102 / % possible obs: 99.9 % / Redundancy: 7.4 % / Rsym value: 4.9 / Net I/σ(I): 35.6 |
Reflection shell | Resolution: 1.8→1.82 Å / Redundancy: 7.1 % / Mean I/σ(I) obs: 5.6 / Rsym value: 36.2 / % possible all: 99.8 |
Reflection | *PLUS Num. measured all: 104415 / Rmerge(I) obs: 0.049 |
Reflection shell | *PLUS % possible obs: 99.8 % |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 1.8→10 Å / σ(F): 2 / ESU R: 0.19
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Displacement parameters | Biso mean: 30.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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