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- PDB-2w9y: The structure of the lipid binding protein Ce-FAR-7 from Caenorha... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2w9y | ||||||
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Title | The structure of the lipid binding protein Ce-FAR-7 from Caenorhabditis elegans | ||||||
![]() | FATTY ACID/RETINOL BINDING PROTEIN PROTEIN 7, ISOFORM A, CONFIRMED BY TRANSCRIPT EVIDENCE | ||||||
![]() | LIPID TRANSPORT / FATTY ACID AND RETINOID BINDING | ||||||
Function / homology | Four Helix Bundle (Hemerythrin (Met), subunit A) - #1100 / Nematode fatty acid retinoid binding / Nematode fatty acid retinoid binding protein (Gp-FAR-1) / oleic acid binding / Four Helix Bundle (Hemerythrin (Met), subunit A) / Up-down Bundle / Mainly Alpha / cytoplasm / Fatty Acid/Retinol binding protein![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Jordanova, R. / Groves, M.R. / Tucker, P.A. | ||||||
![]() | ![]() Title: Fatty Acid and Retinoid Binding Proteins Have Distinct Binding Pockets for the Two Types of Cargo Authors: Jordanova, R. / Groves, M.R. / Kostova, E.B. / Woltersdorf, C. / Liebau, E. / Tucker, P.A. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 71.4 KB | Display | ![]() |
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PDB format | ![]() | 57.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 15542.728 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: RESIDUES GA (N-TERMINUS) ARE FROM THE HIS TAG, C9 IS CSX (CYSTEINE SULFENIC ACID) Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | GA IN THE N-TERMINUS ARE FROM THE HIS TAG, THESE RESIDUES ARE NOT IN Q9TZ51 | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46 % Description: THIS IS THE NATIVE DATASET, USED FOR THE REFINEMENT. THE STRUCTURE WAS SOLVED WITH SESAD FROM THE ADDITIONAL DATASET, GIVEN BELOW. |
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Crystal grow | pH: 7.5 / Details: 20MM TRIS PH 7.8-8.5, 2.1-2.9M AMMONIUM SULFATE |
-Data collection
Diffraction |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 1.79→50 Å / Num. obs: 13757 / % possible obs: 97.7 % / Observed criterion σ(I): -3 / Redundancy: 3.4 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 10.13 | ||||||||||||||||||
Reflection shell | Resolution: 1.79→1.9 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.59 / Mean I/σ(I) obs: 2.19 / % possible all: 94.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 1.8→50.9 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.917 / SU B: 6.542 / SU ML: 0.092 / Cross valid method: THROUGHOUT / ESU R: 0.275 / ESU R Free: 0.143 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 42, 43, 44 AND 45 ARE DISORDERED
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.44 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→50.9 Å
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Refine LS restraints |
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