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Yorodumi- PDB-1hmr: 1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hmr | ||||||
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Title | 1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS | ||||||
Components | MUSCLE FATTY ACID BINDING PROTEIN | ||||||
Keywords | LIPID BINDING PROTEIN / LIPID-BINDING PROTEIN | ||||||
Function / homology | Function and homology information positive regulation of long-chain fatty acid import into cell / regulation of phosphatidylcholine biosynthetic process / regulation of fatty acid oxidation / positive regulation of phospholipid biosynthetic process / intracellular lipid transport / oleic acid binding / phospholipid homeostasis / long-chain fatty acid binding / Triglyceride catabolism / long-chain fatty acid transport ...positive regulation of long-chain fatty acid import into cell / regulation of phosphatidylcholine biosynthetic process / regulation of fatty acid oxidation / positive regulation of phospholipid biosynthetic process / intracellular lipid transport / oleic acid binding / phospholipid homeostasis / long-chain fatty acid binding / Triglyceride catabolism / long-chain fatty acid transport / brown fat cell differentiation / cytoskeletal protein binding / cholesterol homeostasis / negative regulation of cell population proliferation / extracellular space / extracellular exosome / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.4 Å | ||||||
Authors | Young, A.C.M. / Scapin, G. / Kromminga, A. / Patel, S.B. / Veerkamp, J.H. / Sacchettini, J.C. | ||||||
Citation | Journal: Structure / Year: 1994 Title: Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids. Authors: Young, A.C. / Scapin, G. / Kromminga, A. / Patel, S.B. / Veerkamp, J.H. / Sacchettini, J.C. #1: Journal: J.Biol.Chem. / Year: 1992 Title: Three-Dimensional Structure of Recombinant Human Muscle Fatty-Acid Binding Protein Authors: Zanotti, G. / Scapin, G. / Spadon, P. / Weerkamp, J.H. / Sacchettini, J.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hmr.cif.gz | 41.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hmr.ent.gz | 28.1 KB | Display | PDB format |
PDBx/mmJSON format | 1hmr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1hmr_validation.pdf.gz | 408.3 KB | Display | wwPDB validaton report |
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Full document | 1hmr_full_validation.pdf.gz | 412.6 KB | Display | |
Data in XML | 1hmr_validation.xml.gz | 5.2 KB | Display | |
Data in CIF | 1hmr_validation.cif.gz | 8.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hm/1hmr ftp://data.pdbj.org/pub/pdb/validation_reports/hm/1hmr | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14747.825 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P05413 |
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#2: Chemical | ChemComp-ELA / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47.01 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.1 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.36 Å / Lowest resolution: 35.8 Å / Num. obs: 26005 / % possible obs: 83.4 % / Num. measured all: 92367 / Rmerge(I) obs: 0.1 |
-Processing
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Refinement | Resolution: 1.4→8 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.4→8 Å
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Refine LS restraints |
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